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Database: PDB
Entry: 5Y2Z
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HEADER    CELL ADHESION                           27-JUL-17   5Y2Z              
TITLE     CRYSTAL STRUCTURE OF HUMAN LGI1 EPTP-ADAM22 COMPLEX                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN
COMPND   3 22;                                                                  
COMPND   4 CHAIN: A, C, E, G, I, K;                                             
COMPND   5 FRAGMENT: UNP RESIDUES 233-729;                                      
COMPND   6 SYNONYM: ADAM 22,METALLOPROTEINASE-DISINTEGRIN ADAM22-3,             
COMPND   7 METALLOPROTEINASE-LIKE,DISINTEGRIN-LIKE,AND CYSTEINE-RICH PROTEIN 2; 
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: LEUCINE-RICH GLIOMA-INACTIVATED PROTEIN 1;                 
COMPND  11 CHAIN: B, D, F, H, J, L;                                             
COMPND  12 FRAGMENT: UNP RESIDUES 224-557;                                      
COMPND  13 SYNONYM: EPITEMPIN-1;                                                
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ADAM22, MDC2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: MAMMALIA;                                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 40674;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: LGI1, EPT, UNQ775/PRO1569;                                     
SOURCE  13 EXPRESSION_SYSTEM: MAMMALIA;                                         
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 40674                                       
KEYWDS    EPILEPSY, SYNAPSE, ADAM, EPTP, WD40, CELL ADHESION                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.YAMAGATA,S.FUKAI                                                    
REVDAT   2   31-OCT-18 5Y2Z    1       TITLE                                    
REVDAT   1   02-MAY-18 5Y2Z    0                                                
JRNL        AUTH   A.YAMAGATA,Y.MIYAZAKI,N.YOKOI,H.SHIGEMATSU,Y.SATO,           
JRNL        AUTH 2 S.GOTO-ITO,A.MAEDA,T.GOTO,M.SANBO,M.HIRABAYASHI,M.SHIROUZU,  
JRNL        AUTH 3 Y.FUKATA,M.FUKATA,S.FUKAI                                    
JRNL        TITL   STRUCTURAL BASIS OF EPILEPSY-RELATED LIGAND-RECEPTOR COMPLEX 
JRNL        TITL 2 LGI1-ADAM22.                                                 
JRNL        REF    NAT COMMUN                    V.   9  1546 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29670100                                                     
JRNL        DOI    10.1038/S41467-018-03947-W                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.67 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.67                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.040                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 177245                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9033                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.8356 -  8.2712    0.93     5830   224  0.2409 0.2783        
REMARK   3     2  8.2712 -  6.5702    0.87     5349   320  0.2345 0.2375        
REMARK   3     3  6.5702 -  5.7411    0.93     5785   340  0.2281 0.2693        
REMARK   3     4  5.7411 -  5.2169    0.95     5765   332  0.2222 0.2581        
REMARK   3     5  5.2169 -  4.8433    0.84     5270   303  0.2070 0.2408        
REMARK   3     6  4.8433 -  4.5580    0.90     5554   329  0.2020 0.2276        
REMARK   3     7  4.5580 -  4.3299    0.92     5776   266  0.2160 0.2418        
REMARK   3     8  4.3299 -  4.1415    0.93     5763   291  0.2196 0.2314        
REMARK   3     9  4.1415 -  3.9821    0.94     5752   362  0.2274 0.2546        
REMARK   3    10  3.9821 -  3.8448    0.90     5642   307  0.2359 0.2899        
REMARK   3    11  3.8448 -  3.7246    0.85     5255   278  0.2377 0.2713        
REMARK   3    12  3.7246 -  3.6182    0.90     5450   302  0.2420 0.2838        
REMARK   3    13  3.6182 -  3.5229    0.91     5659   354  0.2369 0.2631        
REMARK   3    14  3.5229 -  3.4370    0.91     5645   341  0.2447 0.2844        
REMARK   3    15  3.4370 -  3.3589    0.93     5619   337  0.2534 0.3094        
REMARK   3    16  3.3589 -  3.2874    0.93     5928   228  0.2660 0.3363        
REMARK   3    17  3.2874 -  3.2217    0.94     5678   310  0.2708 0.3197        
REMARK   3    18  3.2217 -  3.1609    0.93     5983   220  0.2777 0.3019        
REMARK   3    19  3.1609 -  3.1045    0.82     4970   303  0.2742 0.3100        
REMARK   3    20  3.1045 -  3.0518    0.87     5579   226  0.2725 0.3429        
REMARK   3    21  3.0518 -  3.0026    0.88     5353   300  0.2772 0.3061        
REMARK   3    22  3.0026 -  2.9564    0.90     5589   273  0.2798 0.3282        
REMARK   3    23  2.9564 -  2.9130    0.90     5626   302  0.2853 0.2980        
REMARK   3    24  2.9130 -  2.8719    0.91     5500   339  0.2863 0.3469        
REMARK   3    25  2.8719 -  2.8331    0.91     5724   367  0.2728 0.3113        
REMARK   3    26  2.8331 -  2.7963    0.92     5588   285  0.2757 0.3184        
REMARK   3    27  2.7963 -  2.7614    0.92     5820   280  0.2778 0.3433        
REMARK   3    28  2.7614 -  2.7281    0.93     5784   289  0.2918 0.3394        
REMARK   3    29  2.7281 -  2.6964    0.92     5532   301  0.2934 0.3147        
REMARK   3    30  2.6964 -  2.6661    0.86     5444   324  0.3047 0.3594        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.420           
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      :  0.005          39615                                  
REMARK   3   ANGLE     :  0.777          53154                                  
REMARK   3   CHIRALITY :  0.036           5837                                  
REMARK   3   PLANARITY :  0.004           6810                                  
REMARK   3   DIHEDRAL  : 12.632          14426                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1197  -1.3998  -0.5036              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2586 T22:   0.2389                                     
REMARK   3      T33:   0.2522 T12:   0.0252                                     
REMARK   3      T13:  -0.0144 T23:  -0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4726 L22:   0.3657                                     
REMARK   3      L33:   1.6131 L12:   0.1386                                     
REMARK   3      L13:   0.8015 L23:   0.1251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1271 S12:  -0.1598 S13:   0.0664                       
REMARK   3      S21:   0.0056 S22:  -0.0410 S23:   0.1018                       
REMARK   3      S31:  -0.1540 S32:  -0.2045 S33:   0.1042                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'C'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.6881 -27.0929 -98.2658              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2115 T22:   0.2181                                     
REMARK   3      T33:   0.3121 T12:  -0.0096                                     
REMARK   3      T13:   0.0402 T23:  -0.0528                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1963 L22:   2.6703                                     
REMARK   3      L33:   2.1956 L12:  -1.8866                                     
REMARK   3      L13:  -1.2876 L23:   0.6834                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1743 S12:   0.0533 S13:  -0.3867                       
REMARK   3      S21:   0.0541 S22:  -0.0889 S23:   0.1263                       
REMARK   3      S31:   0.3483 S32:  -0.0923 S33:   0.0558                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'E'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.6269  31.9235 -79.4392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1921 T22:   0.2120                                     
REMARK   3      T33:   0.2904 T12:   0.0239                                     
REMARK   3      T13:  -0.0343 T23:  -0.0433                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2150 L22:   2.8274                                     
REMARK   3      L33:   2.3068 L12:   1.7117                                     
REMARK   3      L13:   1.3078 L23:   0.5456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0871 S12:  -0.1172 S13:   0.4199                       
REMARK   3      S21:   0.0224 S22:  -0.1949 S23:   0.0634                       
REMARK   3      S31:  -0.3362 S32:  -0.1174 S33:   0.1093                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'G'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  50.9833 -31.4208  18.3259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2250 T22:   0.2287                                     
REMARK   3      T33:   0.2973 T12:   0.0241                                     
REMARK   3      T13:  -0.0184 T23:   0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5868 L22:   3.8846                                     
REMARK   3      L33:   2.0615 L12:  -1.2958                                     
REMARK   3      L13:  -0.2552 L23:  -1.0700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1396 S12:  -0.0032 S13:  -0.2474                       
REMARK   3      S21:   0.1968 S22:  -0.1613 S23:  -0.2140                       
REMARK   3      S31:   0.0458 S32:   0.3286 S33:   0.1076                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'I'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -41.6782 -65.4160-177.3244              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2429 T22:   0.2789                                     
REMARK   3      T33:   0.2667 T12:  -0.0364                                     
REMARK   3      T13:  -0.0013 T23:  -0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1949 L22:   0.5351                                     
REMARK   3      L33:   1.7430 L12:  -0.4531                                     
REMARK   3      L13:  -1.2773 L23:   0.1803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1418 S12:   0.2865 S13:  -0.0955                       
REMARK   3      S21:  -0.0460 S22:  -0.0606 S23:   0.1897                       
REMARK   3      S31:   0.2207 S32:  -0.2494 S33:   0.0691                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'K'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5867 -35.1211-195.7010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2037 T22:   0.2727                                     
REMARK   3      T33:   0.2824 T12:  -0.0440                                     
REMARK   3      T13:  -0.0408 T23:   0.0335                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0774 L22:   3.5359                                     
REMARK   3      L33:   2.2521 L12:   0.9828                                     
REMARK   3      L13:  -0.1201 L23:  -1.3340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0715 S12:   0.0340 S13:   0.1713                       
REMARK   3      S21:   0.0035 S22:  -0.2608 S23:  -0.2563                       
REMARK   3      S31:  -0.0849 S32:   0.3792 S33:   0.0786                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9616  -0.3145  39.7481              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3019 T22:   0.1978                                     
REMARK   3      T33:   0.1731 T12:   0.0293                                     
REMARK   3      T13:  -0.0670 T23:   0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7707 L22:   1.6869                                     
REMARK   3      L33:   2.0742 L12:   0.0004                                     
REMARK   3      L13:  -0.2160 L23:  -0.6431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1000 S12:  -0.0406 S13:  -0.0264                       
REMARK   3      S21:   0.1548 S22:   0.0176 S23:  -0.0906                       
REMARK   3      S31:  -0.0247 S32:  -0.0329 S33:   0.0358                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'D'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -18.1234  -8.3281 -57.8773              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2436 T22:   0.2256                                     
REMARK   3      T33:   0.1596 T12:   0.0003                                     
REMARK   3      T13:   0.0409 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5362 L22:   2.1366                                     
REMARK   3      L33:   1.6471 L12:   0.0248                                     
REMARK   3      L13:   0.5641 L23:  -0.1383                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0455 S12:  -0.1044 S13:   0.0680                       
REMARK   3      S21:   0.1733 S22:  -0.0620 S23:   0.0262                       
REMARK   3      S31:   0.0348 S32:   0.0162 S33:   0.0144                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'F'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -17.9471  13.5986-119.9753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2251 T22:   0.2197                                     
REMARK   3      T33:   0.2013 T12:   0.0224                                     
REMARK   3      T13:  -0.0458 T23:  -0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6797 L22:   1.7778                                     
REMARK   3      L33:   1.9776 L12:   0.1942                                     
REMARK   3      L13:  -0.3332 L23:   0.1252                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1027 S12:  -0.0204 S13:  -0.0788                       
REMARK   3      S21:  -0.1212 S22:  -0.1403 S23:   0.0485                       
REMARK   3      S31:  -0.1283 S32:   0.1121 S33:   0.0072                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'H'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  41.6493 -11.4459 -22.3899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2744 T22:   0.3333                                     
REMARK   3      T33:   0.1903 T12:   0.0131                                     
REMARK   3      T13:  -0.0160 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1143 L22:   1.5504                                     
REMARK   3      L33:   1.2524 L12:   0.0552                                     
REMARK   3      L13:   0.1069 L23:   0.3699                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0417 S12:   0.2881 S13:   0.0443                       
REMARK   3      S21:  -0.1752 S22:   0.0159 S23:   0.1726                       
REMARK   3      S31:  -0.0258 S32:  -0.0978 S33:  -0.0488                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'J'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1922 -66.3361-217.6574              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3375 T22:   0.3366                                     
REMARK   3      T33:   0.2103 T12:  -0.0810                                     
REMARK   3      T13:   0.0713 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7482 L22:   2.2486                                     
REMARK   3      L33:   1.8942 L12:   0.1702                                     
REMARK   3      L13:   0.2134 L23:  -0.2956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0634 S12:   0.0486 S13:   0.1761                       
REMARK   3      S21:  -0.2551 S22:   0.0724 S23:  -0.0858                       
REMARK   3      S31:  -0.0770 S32:  -0.0695 S33:  -0.0210                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'L'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.1530 -55.3764-155.4519              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2215 T22:   0.3345                                     
REMARK   3      T33:   0.2267 T12:  -0.0019                                     
REMARK   3      T13:   0.0425 T23:   0.0439                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7356 L22:   1.8184                                     
REMARK   3      L33:   1.7901 L12:  -0.3188                                     
REMARK   3      L13:   0.0785 L23:   0.5136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0683 S12:  -0.3559 S13:  -0.0861                       
REMARK   3      S21:   0.1280 S22:   0.0445 S23:   0.2071                       
REMARK   3      S31:  -0.0705 S32:  -0.1348 S33:  -0.0324                       
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 5Y2Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004587.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 177282                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.670                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.6                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.53000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3G5C                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 8000, 0.1 M ZINC ACETATE, 0.1   
REMARK 280  M MES-NA (PH 6.0), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A   626                                                      
REMARK 465     VAL A   627                                                      
REMARK 465     GLN A   628                                                      
REMARK 465     GLN A   629                                                      
REMARK 465     ASP A   719                                                      
REMARK 465     ASP A   720                                                      
REMARK 465     ALA A   721                                                      
REMARK 465     LYS A   722                                                      
REMARK 465     THR A   723                                                      
REMARK 465     GLY A   724                                                      
REMARK 465     ILE A   725                                                      
REMARK 465     THR A   726                                                      
REMARK 465     LEU A   727                                                      
REMARK 465     SER A   728                                                      
REMARK 465     GLY A   729                                                      
REMARK 465     LYS A   730                                                      
REMARK 465     HIS A   731                                                      
REMARK 465     HIS A   732                                                      
REMARK 465     HIS A   733                                                      
REMARK 465     HIS A   734                                                      
REMARK 465     HIS A   735                                                      
REMARK 465     HIS A   736                                                      
REMARK 465     GLY C   584                                                      
REMARK 465     LYS C   585                                                      
REMARK 465     ASP C   586                                                      
REMARK 465     LYS C   587                                                      
REMARK 465     ASP C   588                                                      
REMARK 465     THR C   589                                                      
REMARK 465     TRP C   590                                                      
REMARK 465     ILE C   591                                                      
REMARK 465     GLN C   592                                                      
REMARK 465     VAL C   627                                                      
REMARK 465     GLN C   628                                                      
REMARK 465     GLN C   629                                                      
REMARK 465     GLY C   630                                                      
REMARK 465     ASP C   719                                                      
REMARK 465     ASP C   720                                                      
REMARK 465     ALA C   721                                                      
REMARK 465     LYS C   722                                                      
REMARK 465     THR C   723                                                      
REMARK 465     GLY C   724                                                      
REMARK 465     ILE C   725                                                      
REMARK 465     THR C   726                                                      
REMARK 465     LEU C   727                                                      
REMARK 465     SER C   728                                                      
REMARK 465     GLY C   729                                                      
REMARK 465     LYS C   730                                                      
REMARK 465     HIS C   731                                                      
REMARK 465     HIS C   732                                                      
REMARK 465     HIS C   733                                                      
REMARK 465     HIS C   734                                                      
REMARK 465     HIS C   735                                                      
REMARK 465     HIS C   736                                                      
REMARK 465     GLY E   584                                                      
REMARK 465     LYS E   585                                                      
REMARK 465     ASP E   586                                                      
REMARK 465     LYS E   587                                                      
REMARK 465     ASP E   588                                                      
REMARK 465     THR E   589                                                      
REMARK 465     TRP E   590                                                      
REMARK 465     ILE E   591                                                      
REMARK 465     GLN E   592                                                      
REMARK 465     THR E   624                                                      
REMARK 465     LEU E   625                                                      
REMARK 465     VAL E   626                                                      
REMARK 465     VAL E   627                                                      
REMARK 465     GLN E   628                                                      
REMARK 465     GLN E   629                                                      
REMARK 465     GLY E   630                                                      
REMARK 465     ARG E   631                                                      
REMARK 465     THR E   632                                                      
REMARK 465     LEU E   633                                                      
REMARK 465     ASP E   719                                                      
REMARK 465     ASP E   720                                                      
REMARK 465     ALA E   721                                                      
REMARK 465     LYS E   722                                                      
REMARK 465     THR E   723                                                      
REMARK 465     GLY E   724                                                      
REMARK 465     ILE E   725                                                      
REMARK 465     THR E   726                                                      
REMARK 465     LEU E   727                                                      
REMARK 465     SER E   728                                                      
REMARK 465     GLY E   729                                                      
REMARK 465     LYS E   730                                                      
REMARK 465     HIS E   731                                                      
REMARK 465     HIS E   732                                                      
REMARK 465     HIS E   733                                                      
REMARK 465     HIS E   734                                                      
REMARK 465     HIS E   735                                                      
REMARK 465     HIS E   736                                                      
REMARK 465     GLY G   584                                                      
REMARK 465     LYS G   585                                                      
REMARK 465     ASP G   586                                                      
REMARK 465     LYS G   587                                                      
REMARK 465     ASP G   588                                                      
REMARK 465     THR G   589                                                      
REMARK 465     TRP G   590                                                      
REMARK 465     ILE G   591                                                      
REMARK 465     GLN G   592                                                      
REMARK 465     GLU G   620                                                      
REMARK 465     ILE G   621                                                      
REMARK 465     THR G   622                                                      
REMARK 465     SER G   623                                                      
REMARK 465     THR G   624                                                      
REMARK 465     LEU G   625                                                      
REMARK 465     VAL G   626                                                      
REMARK 465     VAL G   627                                                      
REMARK 465     GLN G   628                                                      
REMARK 465     GLN G   629                                                      
REMARK 465     GLY G   630                                                      
REMARK 465     ARG G   631                                                      
REMARK 465     THR G   632                                                      
REMARK 465     LEU G   633                                                      
REMARK 465     ASN G   634                                                      
REMARK 465     ASP G   719                                                      
REMARK 465     ASP G   720                                                      
REMARK 465     ALA G   721                                                      
REMARK 465     LYS G   722                                                      
REMARK 465     THR G   723                                                      
REMARK 465     GLY G   724                                                      
REMARK 465     ILE G   725                                                      
REMARK 465     THR G   726                                                      
REMARK 465     LEU G   727                                                      
REMARK 465     SER G   728                                                      
REMARK 465     GLY G   729                                                      
REMARK 465     LYS G   730                                                      
REMARK 465     HIS G   731                                                      
REMARK 465     HIS G   732                                                      
REMARK 465     HIS G   733                                                      
REMARK 465     HIS G   734                                                      
REMARK 465     HIS G   735                                                      
REMARK 465     HIS G   736                                                      
REMARK 465     GLN I   628                                                      
REMARK 465     GLN I   629                                                      
REMARK 465     GLY I   630                                                      
REMARK 465     ARG I   631                                                      
REMARK 465     THR I   632                                                      
REMARK 465     ASP I   719                                                      
REMARK 465     ASP I   720                                                      
REMARK 465     ALA I   721                                                      
REMARK 465     LYS I   722                                                      
REMARK 465     THR I   723                                                      
REMARK 465     GLY I   724                                                      
REMARK 465     ILE I   725                                                      
REMARK 465     THR I   726                                                      
REMARK 465     LEU I   727                                                      
REMARK 465     SER I   728                                                      
REMARK 465     GLY I   729                                                      
REMARK 465     LYS I   730                                                      
REMARK 465     HIS I   731                                                      
REMARK 465     HIS I   732                                                      
REMARK 465     HIS I   733                                                      
REMARK 465     HIS I   734                                                      
REMARK 465     HIS I   735                                                      
REMARK 465     HIS I   736                                                      
REMARK 465     ASP K   719                                                      
REMARK 465     ASP K   720                                                      
REMARK 465     ALA K   721                                                      
REMARK 465     LYS K   722                                                      
REMARK 465     THR K   723                                                      
REMARK 465     GLY K   724                                                      
REMARK 465     ILE K   725                                                      
REMARK 465     THR K   726                                                      
REMARK 465     LEU K   727                                                      
REMARK 465     SER K   728                                                      
REMARK 465     GLY K   729                                                      
REMARK 465     LYS K   730                                                      
REMARK 465     HIS K   731                                                      
REMARK 465     HIS K   732                                                      
REMARK 465     HIS K   733                                                      
REMARK 465     HIS K   734                                                      
REMARK 465     HIS K   735                                                      
REMARK 465     HIS K   736                                                      
REMARK 465     ASP B   218                                                      
REMARK 465     ALA B   219                                                      
REMARK 465     ALA B   220                                                      
REMARK 465     GLN B   221                                                      
REMARK 465     PRO B   222                                                      
REMARK 465     ALA B   223                                                      
REMARK 465     ILE B   552                                                      
REMARK 465     VAL B   553                                                      
REMARK 465     ASP B   554                                                      
REMARK 465     LEU B   555                                                      
REMARK 465     SER B   556                                                      
REMARK 465     ALA B   557                                                      
REMARK 465     LYS B   558                                                      
REMARK 465     HIS B   559                                                      
REMARK 465     HIS B   560                                                      
REMARK 465     HIS B   561                                                      
REMARK 465     HIS B   562                                                      
REMARK 465     HIS B   563                                                      
REMARK 465     HIS B   564                                                      
REMARK 465     ASP D   218                                                      
REMARK 465     ALA D   219                                                      
REMARK 465     ALA D   220                                                      
REMARK 465     GLN D   221                                                      
REMARK 465     PRO D   222                                                      
REMARK 465     ALA D   223                                                      
REMARK 465     ILE D   552                                                      
REMARK 465     VAL D   553                                                      
REMARK 465     ASP D   554                                                      
REMARK 465     LEU D   555                                                      
REMARK 465     SER D   556                                                      
REMARK 465     ALA D   557                                                      
REMARK 465     LYS D   558                                                      
REMARK 465     HIS D   559                                                      
REMARK 465     HIS D   560                                                      
REMARK 465     HIS D   561                                                      
REMARK 465     HIS D   562                                                      
REMARK 465     HIS D   563                                                      
REMARK 465     HIS D   564                                                      
REMARK 465     ASP F   218                                                      
REMARK 465     ALA F   219                                                      
REMARK 465     ALA F   220                                                      
REMARK 465     GLN F   221                                                      
REMARK 465     PRO F   222                                                      
REMARK 465     ALA F   223                                                      
REMARK 465     ILE F   552                                                      
REMARK 465     VAL F   553                                                      
REMARK 465     ASP F   554                                                      
REMARK 465     LEU F   555                                                      
REMARK 465     SER F   556                                                      
REMARK 465     ALA F   557                                                      
REMARK 465     LYS F   558                                                      
REMARK 465     HIS F   559                                                      
REMARK 465     HIS F   560                                                      
REMARK 465     HIS F   561                                                      
REMARK 465     HIS F   562                                                      
REMARK 465     HIS F   563                                                      
REMARK 465     HIS F   564                                                      
REMARK 465     ASP H   218                                                      
REMARK 465     ALA H   219                                                      
REMARK 465     ALA H   220                                                      
REMARK 465     GLN H   221                                                      
REMARK 465     PRO H   222                                                      
REMARK 465     ALA H   223                                                      
REMARK 465     VAL H   553                                                      
REMARK 465     ASP H   554                                                      
REMARK 465     LEU H   555                                                      
REMARK 465     SER H   556                                                      
REMARK 465     ALA H   557                                                      
REMARK 465     LYS H   558                                                      
REMARK 465     HIS H   559                                                      
REMARK 465     HIS H   560                                                      
REMARK 465     HIS H   561                                                      
REMARK 465     HIS H   562                                                      
REMARK 465     HIS H   563                                                      
REMARK 465     HIS H   564                                                      
REMARK 465     ASP J   218                                                      
REMARK 465     ALA J   219                                                      
REMARK 465     ALA J   220                                                      
REMARK 465     GLN J   221                                                      
REMARK 465     PRO J   222                                                      
REMARK 465     ALA J   223                                                      
REMARK 465     ILE J   552                                                      
REMARK 465     VAL J   553                                                      
REMARK 465     ASP J   554                                                      
REMARK 465     LEU J   555                                                      
REMARK 465     SER J   556                                                      
REMARK 465     ALA J   557                                                      
REMARK 465     LYS J   558                                                      
REMARK 465     HIS J   559                                                      
REMARK 465     HIS J   560                                                      
REMARK 465     HIS J   561                                                      
REMARK 465     HIS J   562                                                      
REMARK 465     HIS J   563                                                      
REMARK 465     HIS J   564                                                      
REMARK 465     ASP L   218                                                      
REMARK 465     ALA L   219                                                      
REMARK 465     ALA L   220                                                      
REMARK 465     GLN L   221                                                      
REMARK 465     PRO L   222                                                      
REMARK 465     ALA L   223                                                      
REMARK 465     ILE L   552                                                      
REMARK 465     VAL L   553                                                      
REMARK 465     ASP L   554                                                      
REMARK 465     LEU L   555                                                      
REMARK 465     SER L   556                                                      
REMARK 465     ALA L   557                                                      
REMARK 465     LYS L   558                                                      
REMARK 465     HIS L   559                                                      
REMARK 465     HIS L   560                                                      
REMARK 465     HIS L   561                                                      
REMARK 465     HIS L   562                                                      
REMARK 465     HIS L   563                                                      
REMARK 465     HIS L   564                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN J   422     O2   FUC J   604              1.31            
REMARK 500   O    TYR H   377     O    HOH H   701              1.81            
REMARK 500   O    TYR B   377     O    HOH B   701              1.81            
REMARK 500   O    HOH J   742     O    HOH J   746              1.81            
REMARK 500   O    HOH E   974     O    HOH E   977              1.82            
REMARK 500   O    HOH E   906     O    HOH E   922              1.83            
REMARK 500   OD1  ASP H   381     O    HOH H   702              1.84            
REMARK 500   OE1  GLU K   665     O    HOH K   901              1.84            
REMARK 500   O4   NAG F   605     O    HOH F   701              1.85            
REMARK 500   O    TYR C   409     O    HOH C   901              1.85            
REMARK 500   OE1  GLU I   322     O    HOH I   901              1.85            
REMARK 500   NH1  ARG E   513     O    HOH E   901              1.85            
REMARK 500   O    GLU B   325     O    HOH B   702              1.85            
REMARK 500   O    HOH H   756     O    HOH H   757              1.86            
REMARK 500   O    VAL B   519     O    HOH B   703              1.87            
REMARK 500   O    HOH I   932     O    HOH I   956              1.87            
REMARK 500   O    VAL E   598     O    HOH E   902              1.88            
REMARK 500   O    CYS E   401     O    HOH E   903              1.90            
REMARK 500   NE2  HIS L   307     O    HOH L   701              1.91            
REMARK 500   O    GLY J   366     O    HOH J   701              1.91            
REMARK 500   NZ   LYS K   253     O    HOH K   902              1.92            
REMARK 500   OG   SER A   695     O    HOH A   901              1.93            
REMARK 500   O    HOH E   958     O    HOH F   756              1.94            
REMARK 500   O    HOH G   953     O    HOH G   954              1.94            
REMARK 500   O    HOH I   906     O    HOH I   969              1.95            
REMARK 500   O    GLY G   430     O    HOH G   901              1.95            
REMARK 500   OG1  THR A   624     O    HOH A   902              1.95            
REMARK 500   O    PHE E   451     OE1  GLU E   456              1.96            
REMARK 500   O    GLN B   301     O    HOH B   704              1.96            
REMARK 500   NZ   LYS H   459     O    HOH H   703              1.97            
REMARK 500   OG   SER K   389     O    HOH K   903              1.97            
REMARK 500   OD2  ASP K   551     O    HOH K   904              1.97            
REMARK 500   OE2  GLU G   420     O    HOH G   902              1.98            
REMARK 500   OD1  ASP B   381     O    HOH B   705              1.98            
REMARK 500   O    GLY B   461     O    HOH B   706              1.99            
REMARK 500   OE2  GLU K   237     O    HOH K   905              1.99            
REMARK 500   O    PRO A   463     O    HOH A   903              1.99            
REMARK 500   OH   TYR K   602     O    HOH K   906              1.99            
REMARK 500   O    VAL L   519     O    HOH L   702              1.99            
REMARK 500   O    HOH C   967     O    HOH F   707              2.00            
REMARK 500   O    GLU I   456     O    HOH I   902              2.00            
REMARK 500   NE2  HIS B   307     O    HOH B   707              2.00            
REMARK 500   OD1  ASN G   703     O    HOH G   903              2.01            
REMARK 500   O    PRO K   444     O    HOH K   907              2.01            
REMARK 500   O    HOH A   969     O    HOH A   982              2.01            
REMARK 500   O    SER A   399     O    HOH A   904              2.01            
REMARK 500   NZ   LYS G   253     O    HOH G   904              2.01            
REMARK 500   O    HOH E   921     O    HOH E   969              2.01            
REMARK 500   O    HOH K   905     O    HOH K   951              2.02            
REMARK 500   NZ   LYS C   561     O    HOH C   902              2.02            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     183 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH K   959     O    HOH B   783     1554     1.93            
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    GLU C 514   CB    GLU C 514   CG      0.123                       
REMARK 500    PHE B 498   CD1   PHE B 498   CE1    -0.144                       
REMARK 500    GLU B 516   CG    GLU B 516   CD     -0.103                       
REMARK 500    GLU B 516   CD    GLU B 516   OE1    -0.116                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 474   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    PHE B 498   CD1 -  CE1 -  CZ  ANGL. DEV. =   7.3 DEGREES          
REMARK 500    GLU B 516   CG  -  CD  -  OE1 ANGL. DEV. = -14.6 DEGREES          
REMARK 500    GLU B 516   CG  -  CD  -  OE2 ANGL. DEV. =  16.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 336       33.63    -96.66                                   
REMARK 500    CYS A 349       -0.64     71.58                                   
REMARK 500    SER A 439      -74.38   -111.36                                   
REMARK 500    ASP A 459       95.79   -164.55                                   
REMARK 500    ASP A 482       64.79   -112.20                                   
REMARK 500    CYS A 583       40.53   -108.08                                   
REMARK 500    LYS A 587       73.22     51.02                                   
REMARK 500    ASP A 597       33.12    -87.55                                   
REMARK 500    GLU C 336       34.15    -97.03                                   
REMARK 500    CYS C 349       -0.36     71.47                                   
REMARK 500    SER C 439      -74.15   -111.60                                   
REMARK 500    GLU C 453     -169.83   -100.79                                   
REMARK 500    ASP C 459       91.32   -164.41                                   
REMARK 500    ASP C 482       65.10   -115.03                                   
REMARK 500    ASP C 597       33.56    -92.39                                   
REMARK 500    ASN C 634       72.89    -66.16                                   
REMARK 500    GLU E 336       34.11    -96.92                                   
REMARK 500    CYS E 349       -0.02     71.71                                   
REMARK 500    SER E 439      -73.65   -111.58                                   
REMARK 500    GLU E 453     -169.97   -102.19                                   
REMARK 500    ASP E 459       92.11   -161.92                                   
REMARK 500    ASP E 482       67.53   -114.56                                   
REMARK 500    ASP E 597       32.55    -86.57                                   
REMARK 500    GLU G 336       34.10    -95.92                                   
REMARK 500    SER G 439      -73.14   -111.62                                   
REMARK 500    ASP G 459       90.95   -163.58                                   
REMARK 500    ASP G 482       62.39   -108.06                                   
REMARK 500    ASP G 597       32.84    -87.80                                   
REMARK 500    GLU I 336       33.50    -95.92                                   
REMARK 500    CYS I 349       -1.25     71.74                                   
REMARK 500    ASP I 383      106.70    -58.97                                   
REMARK 500    SER I 439      -73.05   -111.23                                   
REMARK 500    ASP I 459       97.62   -164.48                                   
REMARK 500    ASP I 482       64.12   -113.65                                   
REMARK 500    LYS I 587       72.21     52.72                                   
REMARK 500    ASP I 597       32.68    -92.84                                   
REMARK 500    HIS I 717       18.90   -154.87                                   
REMARK 500    GLU K 336       33.64    -97.28                                   
REMARK 500    ASP K 383      105.31    -59.73                                   
REMARK 500    SER K 439      -73.11   -111.74                                   
REMARK 500    ASP K 459       94.02   -165.72                                   
REMARK 500    ASP K 482       60.41   -110.21                                   
REMARK 500    LYS K 587       74.40     51.35                                   
REMARK 500    ASP K 597       33.28    -86.57                                   
REMARK 500    GLN K 629       35.60     39.53                                   
REMARK 500    PRO B 233       50.38    -68.79                                   
REMARK 500    LEU B 237      -63.62   -109.15                                   
REMARK 500    THR B 257      -61.04    -91.68                                   
REMARK 500    GLU B 341       66.27     37.03                                   
REMARK 500    ASN B 342       16.78     59.14                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      79 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 991        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH G 969        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH G 970        DISTANCE =  7.60 ANGSTROMS                       
REMARK 525    HOH G 971        DISTANCE =  8.92 ANGSTROMS                       
REMARK 525    HOH G 972        DISTANCE = 10.83 ANGSTROMS                       
REMARK 525    HOH I 990        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH I 991        DISTANCE =  7.02 ANGSTROMS                       
REMARK 525    HOH F 762        DISTANCE =  5.82 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 242   OE2                                                    
REMARK 620 2 ASP A 325   OD1  91.2                                              
REMARK 620 3 ASP A 325   OD2  96.5  54.6                                        
REMARK 620 4 CYS A 433   O   167.3  77.3  81.4                                  
REMARK 620 5 ASN A 436   OD1 118.9 129.4 142.7  66.5                            
REMARK 620 6 HOH A 934   O    80.9  64.1 118.6  89.2  80.7                      
REMARK 620 7 HOH A 921   O   110.2 122.4  69.8  80.9  86.3 166.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 446   O                                                      
REMARK 620 2 ASN A 449   OD1  79.4                                              
REMARK 620 3 PHE A 451   O   157.8  80.5                                        
REMARK 620 4 GLU A 453   OE1  92.5 121.0 106.0                                  
REMARK 620 5 GLU A 456   OE1 121.3 130.9  67.0 103.3                            
REMARK 620 6 ASP A 459   OD2  82.3  66.6  81.1 170.0  72.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 511   OD1                                                    
REMARK 620 2 ASP A 511   OD2  54.7                                              
REMARK 620 3 ILE A 512   O    96.5  95.1                                        
REMARK 620 4 GLU A 514   OE2 142.2 161.5  77.5                                  
REMARK 620 5 ASN A 526   OD1 100.4 106.0 158.1  80.6                            
REMARK 620 6 ILE A 527   O    70.4 124.9  85.7  72.0  86.9                      
REMARK 620 7 HOH A 911   O   105.2  50.5  91.1 112.1  97.8 174.2                
REMARK 620 8 HOH A 926   O   145.8  99.0 108.5  68.1  63.1 132.9  52.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 242   OE2                                                    
REMARK 620 2 ASP C 325   OD1  91.7                                              
REMARK 620 3 ASP C 325   OD2  95.6  54.6                                        
REMARK 620 4 CYS C 433   O   170.3  79.0  81.5                                  
REMARK 620 5 ASN C 436   OD1 119.5 129.0 143.0  65.7                            
REMARK 620 6 HOH C 914   O    98.6  57.7 111.0  74.1  77.3                      
REMARK 620 7 HOH C 941   O   109.9 128.9  76.9  78.5  79.9 149.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 446   O                                                      
REMARK 620 2 ASN C 449   OD1  79.9                                              
REMARK 620 3 PHE C 451   O   152.3  72.4                                        
REMARK 620 4 GLU C 453   OE1  87.3 111.4 103.2                                  
REMARK 620 5 GLU C 456   OE1 145.9 119.5  54.9 107.9                            
REMARK 620 6 GLU C 456   OE2  92.8 144.8 109.4 102.5  54.7                      
REMARK 620 7 ASP C 459   OD2  84.8  66.4  83.5 172.1  79.3  78.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 511   OD1                                                    
REMARK 620 2 ASP C 511   OD2  53.6                                              
REMARK 620 3 ILE C 512   O    84.4  89.3                                        
REMARK 620 4 GLU C 514   OE2 112.6 165.6  84.9                                  
REMARK 620 5 ASN C 526   OD1  90.8  96.4 168.4  87.2                            
REMARK 620 6 ILE C 527   O    55.0 108.5  87.2  58.1  81.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 242   OE2                                                    
REMARK 620 2 ASP E 325   OD1  90.0                                              
REMARK 620 3 ASP E 325   OD2 106.4  54.9                                        
REMARK 620 4 CYS E 433   O   149.4  73.2  84.9                                  
REMARK 620 5 ASN E 436   OD1 113.4 118.9 139.9  58.1                            
REMARK 620 6 HOH E 936   O   124.7 130.8  80.3  84.7  81.2                      
REMARK 620 7 HOH E 935   O    75.5  70.0 124.7  74.8  63.8 144.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 446   O                                                      
REMARK 620 2 ASN E 449   OD1  66.5                                              
REMARK 620 3 PHE E 451   O   133.7  67.3                                        
REMARK 620 4 GLU E 453   OE1  98.5 109.2  93.3                                  
REMARK 620 5 GLU E 456   OE1 155.7 107.1  48.7 105.7                            
REMARK 620 6 GLU E 456   OE2 112.0 141.2 105.7 109.4  57.1                      
REMARK 620 7 ASP E 459   OD2  83.3  59.9  76.7 167.3  73.7  81.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 511   OD1                                                    
REMARK 620 2 ASP E 511   OD2  54.5                                              
REMARK 620 3 ILE E 512   O   102.3  95.6                                        
REMARK 620 4 GLU E 514   OE2 153.5 151.6  76.4                                  
REMARK 620 5 ASN E 526   OD1 101.1 102.1 156.0  80.5                            
REMARK 620 6 ILE E 527   O    74.6 128.8  89.7  79.0  91.7                      
REMARK 620 7 HOH E 906   O    99.6  45.5  80.8 106.1 100.1 167.7                
REMARK 620 8 HOH E 922   O   134.4  83.1  62.3  69.0 103.7 141.1  38.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 242   OE2                                                    
REMARK 620 2 ASP G 325   OD1  85.8                                              
REMARK 620 3 ASP G 325   OD2 102.0  54.9                                        
REMARK 620 4 CYS G 433   O   148.0  73.6  86.2                                  
REMARK 620 5 ASN G 436   OD1 113.5 120.9 144.1  61.0                            
REMARK 620 6 HOH G 922   O   126.7 133.5  83.6  84.7  79.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 446   O                                                      
REMARK 620 2 ASN G 449   OD1  75.5                                              
REMARK 620 3 PHE G 451   O   148.6  73.1                                        
REMARK 620 4 GLU G 453   OE1  87.8 107.2  99.3                                  
REMARK 620 5 GLU G 456   OE1 151.2 120.0  54.4 107.9                            
REMARK 620 6 GLU G 456   OE2  98.7 147.6 108.9 104.4  54.7                      
REMARK 620 7 ASP G 459   OD2  86.6  69.4  84.5 174.1  78.0  78.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 511   OD1                                                    
REMARK 620 2 ASP G 511   OD2  55.2                                              
REMARK 620 3 ILE G 512   O    98.2  92.2                                        
REMARK 620 4 GLU G 514   OE2 142.3 161.9  81.3                                  
REMARK 620 5 ASN G 526   OD1 100.7 106.2 159.0  78.0                            
REMARK 620 6 ILE G 527   O    66.5 121.4  90.3  75.8  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA I 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU I 242   OE2                                                    
REMARK 620 2 ASP I 325   OD1  86.0                                              
REMARK 620 3 ASP I 325   OD2 108.2  54.9                                        
REMARK 620 4 CYS I 433   O   147.0  74.6  82.3                                  
REMARK 620 5 ASN I 436   OD1 111.7 119.7 139.2  59.5                            
REMARK 620 6 HOH I 928   O    69.0  64.0 118.8  78.4  69.9                      
REMARK 620 7 HOH I 930   O   126.8 133.8  81.9  85.1  81.2 151.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA I 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU I 446   O                                                      
REMARK 620 2 ASN I 449   OD1  76.7                                              
REMARK 620 3 PHE I 451   O   151.4  75.0                                        
REMARK 620 4 GLU I 453   OE1  86.3 109.5  99.4                                  
REMARK 620 5 GLU I 456   OE1 152.3 120.8  52.8 105.1                            
REMARK 620 6 GLU I 456   OE2  98.5 147.8 107.5 101.8  54.8                      
REMARK 620 7 ASP I 459   OD2  88.6  66.8  84.0 174.3  80.6  81.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA I 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 511   OD1                                                    
REMARK 620 2 ASP I 511   OD2  55.1                                              
REMARK 620 3 ILE I 512   O   102.0  97.9                                        
REMARK 620 4 GLU I 514   OE2 144.5 160.2  77.7                                  
REMARK 620 5 ASN I 526   OD1  99.2 105.9 154.4  76.7                            
REMARK 620 6 ILE I 527   O    70.9 125.7  87.0  73.7  86.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA K 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU K 242   OE2                                                    
REMARK 620 2 ASP K 325   OD1  92.5                                              
REMARK 620 3 ASP K 325   OD2  95.3  54.8                                        
REMARK 620 4 CYS K 433   O   174.2  81.9  82.6                                  
REMARK 620 5 ASN K 436   OD1 118.5 132.7 142.1  65.2                            
REMARK 620 6 HOH K 941   O    89.1  65.4 120.2  87.3  79.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA K 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU K 446   O                                                      
REMARK 620 2 ASN K 449   OD1  72.9                                              
REMARK 620 3 PHE K 451   O   146.5  73.7                                        
REMARK 620 4 GLU K 453   OE1  89.4 110.0 100.6                                  
REMARK 620 5 GLU K 456   OE1 150.6 118.6  54.1 109.2                            
REMARK 620 6 GLU K 456   OE2  99.4 144.2 108.6 104.7  54.6                      
REMARK 620 7 ASP K 459   OD2  87.0  68.2  82.1 176.3  74.5  76.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA K 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP K 511   OD1                                                    
REMARK 620 2 ASP K 511   OD2  54.7                                              
REMARK 620 3 ILE K 512   O    98.4  94.7                                        
REMARK 620 4 GLU K 514   OE2 145.9 157.8  76.4                                  
REMARK 620 5 ASN K 526   OD1 104.4 106.4 155.1  79.2                            
REMARK 620 6 ILE K 527   O    72.8 127.4  88.3  73.3  89.2                      
REMARK 620 7 HOH K 925   O   111.6  57.5  95.0 102.5  85.7 174.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 334   OD1                                                    
REMARK 620 2 ASP B 334   OD2  53.8                                              
REMARK 620 3 GLU B 336   OE1  80.8  79.1                                        
REMARK 620 4 ASP B 381   OD1  90.0  96.8 170.6                                  
REMARK 620 5 ASP B 381   OD2 136.3 100.6 133.6  55.2                            
REMARK 620 6 VAL B 382   O   126.8  77.8  68.4 119.2  66.3                      
REMARK 620 7 HOH B 705   O    85.4 130.2 125.6  51.3  90.2 147.8                
REMARK 620 8 HOH B 724   O   156.1 147.9  93.3  94.5  62.5  70.5  79.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 334   OD1                                                    
REMARK 620 2 ASP D 334   OD2  55.0                                              
REMARK 620 3 GLU D 336   OE1  82.4  88.4                                        
REMARK 620 4 ASP D 381   OD1  86.4  89.9 167.4                                  
REMARK 620 5 ASP D 381   OD2 132.0  93.7 137.5  55.0                            
REMARK 620 6 VAL D 382   O   126.8  77.7  72.3 119.4  66.8                      
REMARK 620 7 HOH D 715   O    57.5 110.6  97.6  71.4 120.9 167.1                
REMARK 620 8 HOH D 710   O   160.6 144.0  93.2  95.4  61.8  68.7 104.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 334   OD1                                                    
REMARK 620 2 ASP F 334   OD2  55.0                                              
REMARK 620 3 GLU F 336   OE1  84.0  85.9                                        
REMARK 620 4 ASP F 381   OD1  85.9  93.1 168.3                                  
REMARK 620 5 ASP F 381   OD2 132.0  96.3 136.5  55.2                            
REMARK 620 6 VAL F 382   O   128.8  77.9  73.0 118.1  65.1                      
REMARK 620 7 HOH F 706   O    88.6 131.6 124.5  49.3  85.5 141.9                
REMARK 620 8 HOH F 715   O   161.1 143.5  99.5  88.2  55.4  69.5  74.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 334   OD1                                                    
REMARK 620 2 ASP H 334   OD2  54.5                                              
REMARK 620 3 GLU H 336   OE1  81.2  87.9                                        
REMARK 620 4 ASP H 381   OD1  85.5  87.1 166.2                                  
REMARK 620 5 ASP H 381   OD2 130.1  90.9 138.0  54.9                            
REMARK 620 6 VAL H 382   O   123.8  74.7  73.8 117.0  65.5                      
REMARK 620 7 HOH H 715   O   156.2 143.4 110.1  81.2  54.2  80.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA J 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP J 334   OD1                                                    
REMARK 620 2 ASP J 334   OD2  54.9                                              
REMARK 620 3 GLU J 336   OE1  86.6  88.2                                        
REMARK 620 4 ASP J 381   OD1  88.8  94.4 172.1                                  
REMARK 620 5 ASP J 381   OD2 133.7  96.3 132.3  54.9                            
REMARK 620 6 VAL J 382   O   130.1  79.7  70.9 116.8  63.3                      
REMARK 620 7 HOH J 705   O   144.1 155.1  79.5 100.8  77.0  75.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA L 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L 334   OD1                                                    
REMARK 620 2 ASP L 334   OD2  55.0                                              
REMARK 620 3 GLU L 336   OE1  81.0  85.7                                        
REMARK 620 4 ASP L 381   OD1  89.3  95.9 167.0                                  
REMARK 620 5 ASP L 381   OD2 134.4  97.4 137.7  55.0                            
REMARK 620 6 VAL L 382   O   128.7  78.6  74.4 118.5  65.0                      
REMARK 620 7 HOH L 712   O   153.6 149.2 105.8  79.3  54.8  77.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA I 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA I 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA I 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA K 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA K 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA K 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA J 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA L 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  602 through NAG B 603 bound to ASN B 277                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B    
REMARK 800  604 through BMA B 607 bound to ASN B 422                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  602 through NAG D 603 bound to ASN D 277                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC D    
REMARK 800  604 through NAG D 606 bound to ASN D 422                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG F    
REMARK 800  602 through NAG F 603 bound to ASN F 277                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC F    
REMARK 800  604 through NAG F 605 bound to ASN F 422                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG H 602 bound   
REMARK 800  to ASN H 277                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC H    
REMARK 800  603 through BMA H 606 bound to ASN H 422                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG J    
REMARK 800  602 through NAG J 603 bound to ASN J 277                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC J    
REMARK 800  604 through NAG J 606 bound to ASN J 422                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG L 602 bound   
REMARK 800  to ASN L 277                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC L    
REMARK 800  603 through NAG L 605 bound to ASN L 422                            
DBREF  5Y2Z A  233   729  UNP    Q9P0K1   ADA22_HUMAN    233    729             
DBREF  5Y2Z C  233   729  UNP    Q9P0K1   ADA22_HUMAN    233    729             
DBREF  5Y2Z E  233   729  UNP    Q9P0K1   ADA22_HUMAN    233    729             
DBREF  5Y2Z G  233   729  UNP    Q9P0K1   ADA22_HUMAN    233    729             
DBREF  5Y2Z I  233   729  UNP    Q9P0K1   ADA22_HUMAN    233    729             
DBREF  5Y2Z K  233   729  UNP    Q9P0K1   ADA22_HUMAN    233    729             
DBREF  5Y2Z B  224   557  UNP    O95970   LGI1_HUMAN     224    557             
DBREF  5Y2Z D  224   557  UNP    O95970   LGI1_HUMAN     224    557             
DBREF  5Y2Z F  224   557  UNP    O95970   LGI1_HUMAN     224    557             
DBREF  5Y2Z H  224   557  UNP    O95970   LGI1_HUMAN     224    557             
DBREF  5Y2Z J  224   557  UNP    O95970   LGI1_HUMAN     224    557             
DBREF  5Y2Z L  224   557  UNP    O95970   LGI1_HUMAN     224    557             
SEQADV 5Y2Z LYS A  730  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS A  731  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS A  732  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS A  733  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS A  734  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS A  735  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS A  736  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z LYS C  730  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS C  731  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS C  732  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS C  733  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS C  734  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS C  735  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS C  736  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z LYS E  730  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS E  731  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS E  732  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS E  733  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS E  734  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS E  735  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS E  736  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z LYS G  730  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS G  731  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS G  732  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS G  733  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS G  734  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS G  735  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS G  736  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z LYS I  730  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS I  731  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS I  732  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS I  733  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS I  734  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS I  735  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS I  736  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z LYS K  730  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS K  731  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS K  732  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS K  733  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS K  734  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS K  735  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z HIS K  736  UNP  Q9P0K1              EXPRESSION TAG                 
SEQADV 5Y2Z ASP B  218  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA B  219  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA B  220  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z GLN B  221  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z PRO B  222  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA B  223  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z LYS B  558  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS B  559  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS B  560  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS B  561  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS B  562  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS B  563  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS B  564  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ASP D  218  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA D  219  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA D  220  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z GLN D  221  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z PRO D  222  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA D  223  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z LYS D  558  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS D  559  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS D  560  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS D  561  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS D  562  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS D  563  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS D  564  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ASP F  218  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA F  219  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA F  220  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z GLN F  221  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z PRO F  222  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA F  223  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z LYS F  558  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS F  559  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS F  560  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS F  561  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS F  562  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS F  563  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS F  564  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ASP H  218  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA H  219  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA H  220  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z GLN H  221  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z PRO H  222  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA H  223  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z LYS H  558  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS H  559  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS H  560  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS H  561  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS H  562  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS H  563  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS H  564  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ASP J  218  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA J  219  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA J  220  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z GLN J  221  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z PRO J  222  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA J  223  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z LYS J  558  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS J  559  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS J  560  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS J  561  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS J  562  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS J  563  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS J  564  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ASP L  218  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA L  219  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA L  220  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z GLN L  221  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z PRO L  222  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z ALA L  223  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z LYS L  558  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS L  559  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS L  560  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS L  561  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS L  562  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS L  563  UNP  O95970              EXPRESSION TAG                 
SEQADV 5Y2Z HIS L  564  UNP  O95970              EXPRESSION TAG                 
SEQRES   1 A  504  ASN VAL GLU GLU GLU THR LYS TYR ILE GLU LEU MET ILE          
SEQRES   2 A  504  VAL ASN ASP HIS LEU MET PHE LYS LYS HIS ARG LEU SER          
SEQRES   3 A  504  VAL VAL HIS THR ASN THR TYR ALA LYS SER VAL VAL ASN          
SEQRES   4 A  504  MET ALA ASP LEU ILE TYR LYS ASP GLN LEU LYS THR ARG          
SEQRES   5 A  504  ILE VAL LEU VAL ALA MET GLU THR TRP ALA THR ASP ASN          
SEQRES   6 A  504  LYS PHE ALA ILE SER GLU ASN PRO LEU ILE THR LEU ARG          
SEQRES   7 A  504  GLU PHE MET LYS TYR ARG ARG ASP PHE ILE LYS GLU LYS          
SEQRES   8 A  504  SER ASP ALA VAL HIS LEU PHE SER GLY SER GLN PHE GLU          
SEQRES   9 A  504  SER SER ARG SER GLY ALA ALA TYR ILE GLY GLY ILE CYS          
SEQRES  10 A  504  SER LEU LEU LYS GLY GLY GLY VAL ASN GLU PHE GLY LYS          
SEQRES  11 A  504  THR ASP LEU MET ALA VAL THR LEU ALA GLN SER LEU ALA          
SEQRES  12 A  504  HIS ASN ILE GLY ILE ILE SER ASP LYS ARG LYS LEU ALA          
SEQRES  13 A  504  SER GLY GLU CYS LYS CYS GLU ASP THR TRP SER GLY CYS          
SEQRES  14 A  504  ILE MET GLY ASP THR GLY TYR TYR LEU PRO LYS LYS PHE          
SEQRES  15 A  504  THR GLN CYS ASN ILE GLU GLU TYR HIS ASP PHE LEU ASN          
SEQRES  16 A  504  SER GLY GLY GLY ALA CYS LEU PHE ASN LYS PRO SER LYS          
SEQRES  17 A  504  LEU LEU ASP PRO PRO GLU CYS GLY ASN GLY PHE ILE GLU          
SEQRES  18 A  504  THR GLY GLU GLU CYS ASP CYS GLY THR PRO ALA GLU CYS          
SEQRES  19 A  504  VAL LEU GLU GLY ALA GLU CYS CYS LYS LYS CYS THR LEU          
SEQRES  20 A  504  THR GLN ASP SER GLN CYS SER ASP GLY LEU CYS CYS LYS          
SEQRES  21 A  504  LYS CYS LYS PHE GLN PRO MET GLY THR VAL CYS ARG GLU          
SEQRES  22 A  504  ALA VAL ASN ASP CYS ASP ILE ARG GLU THR CYS SER GLY          
SEQRES  23 A  504  ASN SER SER GLN CYS ALA PRO ASN ILE HIS LYS MET ASP          
SEQRES  24 A  504  GLY TYR SER CYS ASP GLY VAL GLN GLY ILE CYS PHE GLY          
SEQRES  25 A  504  GLY ARG CYS LYS THR ARG ASP ARG GLN CYS LYS TYR ILE          
SEQRES  26 A  504  TRP GLY GLN LYS VAL THR ALA SER ASP LYS TYR CYS TYR          
SEQRES  27 A  504  GLU LYS LEU ASN ILE GLU GLY THR GLU LYS GLY ASN CYS          
SEQRES  28 A  504  GLY LYS ASP LYS ASP THR TRP ILE GLN CYS ASN LYS ARG          
SEQRES  29 A  504  ASP VAL LEU CYS GLY TYR LEU LEU CYS THR ASN ILE GLY          
SEQRES  30 A  504  ASN ILE PRO ARG LEU GLY GLU LEU ASP GLY GLU ILE THR          
SEQRES  31 A  504  SER THR LEU VAL VAL GLN GLN GLY ARG THR LEU ASN CYS          
SEQRES  32 A  504  SER GLY GLY HIS VAL LYS LEU GLU GLU ASP VAL ASP LEU          
SEQRES  33 A  504  GLY TYR VAL GLU ASP GLY THR PRO CYS GLY PRO GLN MET          
SEQRES  34 A  504  MET CYS LEU GLU HIS ARG CYS LEU PRO VAL ALA SER PHE          
SEQRES  35 A  504  ASN PHE SER THR CYS LEU SER SER LYS GLU GLY THR ILE          
SEQRES  36 A  504  CYS SER GLY ASN GLY VAL CYS SER ASN GLU LEU LYS CYS          
SEQRES  37 A  504  VAL CYS ASN ARG HIS TRP ILE GLY SER ASP CYS ASN THR          
SEQRES  38 A  504  TYR PHE PRO HIS ASN ASP ASP ALA LYS THR GLY ILE THR          
SEQRES  39 A  504  LEU SER GLY LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 C  504  ASN VAL GLU GLU GLU THR LYS TYR ILE GLU LEU MET ILE          
SEQRES   2 C  504  VAL ASN ASP HIS LEU MET PHE LYS LYS HIS ARG LEU SER          
SEQRES   3 C  504  VAL VAL HIS THR ASN THR TYR ALA LYS SER VAL VAL ASN          
SEQRES   4 C  504  MET ALA ASP LEU ILE TYR LYS ASP GLN LEU LYS THR ARG          
SEQRES   5 C  504  ILE VAL LEU VAL ALA MET GLU THR TRP ALA THR ASP ASN          
SEQRES   6 C  504  LYS PHE ALA ILE SER GLU ASN PRO LEU ILE THR LEU ARG          
SEQRES   7 C  504  GLU PHE MET LYS TYR ARG ARG ASP PHE ILE LYS GLU LYS          
SEQRES   8 C  504  SER ASP ALA VAL HIS LEU PHE SER GLY SER GLN PHE GLU          
SEQRES   9 C  504  SER SER ARG SER GLY ALA ALA TYR ILE GLY GLY ILE CYS          
SEQRES  10 C  504  SER LEU LEU LYS GLY GLY GLY VAL ASN GLU PHE GLY LYS          
SEQRES  11 C  504  THR ASP LEU MET ALA VAL THR LEU ALA GLN SER LEU ALA          
SEQRES  12 C  504  HIS ASN ILE GLY ILE ILE SER ASP LYS ARG LYS LEU ALA          
SEQRES  13 C  504  SER GLY GLU CYS LYS CYS GLU ASP THR TRP SER GLY CYS          
SEQRES  14 C  504  ILE MET GLY ASP THR GLY TYR TYR LEU PRO LYS LYS PHE          
SEQRES  15 C  504  THR GLN CYS ASN ILE GLU GLU TYR HIS ASP PHE LEU ASN          
SEQRES  16 C  504  SER GLY GLY GLY ALA CYS LEU PHE ASN LYS PRO SER LYS          
SEQRES  17 C  504  LEU LEU ASP PRO PRO GLU CYS GLY ASN GLY PHE ILE GLU          
SEQRES  18 C  504  THR GLY GLU GLU CYS ASP CYS GLY THR PRO ALA GLU CYS          
SEQRES  19 C  504  VAL LEU GLU GLY ALA GLU CYS CYS LYS LYS CYS THR LEU          
SEQRES  20 C  504  THR GLN ASP SER GLN CYS SER ASP GLY LEU CYS CYS LYS          
SEQRES  21 C  504  LYS CYS LYS PHE GLN PRO MET GLY THR VAL CYS ARG GLU          
SEQRES  22 C  504  ALA VAL ASN ASP CYS ASP ILE ARG GLU THR CYS SER GLY          
SEQRES  23 C  504  ASN SER SER GLN CYS ALA PRO ASN ILE HIS LYS MET ASP          
SEQRES  24 C  504  GLY TYR SER CYS ASP GLY VAL GLN GLY ILE CYS PHE GLY          
SEQRES  25 C  504  GLY ARG CYS LYS THR ARG ASP ARG GLN CYS LYS TYR ILE          
SEQRES  26 C  504  TRP GLY GLN LYS VAL THR ALA SER ASP LYS TYR CYS TYR          
SEQRES  27 C  504  GLU LYS LEU ASN ILE GLU GLY THR GLU LYS GLY ASN CYS          
SEQRES  28 C  504  GLY LYS ASP LYS ASP THR TRP ILE GLN CYS ASN LYS ARG          
SEQRES  29 C  504  ASP VAL LEU CYS GLY TYR LEU LEU CYS THR ASN ILE GLY          
SEQRES  30 C  504  ASN ILE PRO ARG LEU GLY GLU LEU ASP GLY GLU ILE THR          
SEQRES  31 C  504  SER THR LEU VAL VAL GLN GLN GLY ARG THR LEU ASN CYS          
SEQRES  32 C  504  SER GLY GLY HIS VAL LYS LEU GLU GLU ASP VAL ASP LEU          
SEQRES  33 C  504  GLY TYR VAL GLU ASP GLY THR PRO CYS GLY PRO GLN MET          
SEQRES  34 C  504  MET CYS LEU GLU HIS ARG CYS LEU PRO VAL ALA SER PHE          
SEQRES  35 C  504  ASN PHE SER THR CYS LEU SER SER LYS GLU GLY THR ILE          
SEQRES  36 C  504  CYS SER GLY ASN GLY VAL CYS SER ASN GLU LEU LYS CYS          
SEQRES  37 C  504  VAL CYS ASN ARG HIS TRP ILE GLY SER ASP CYS ASN THR          
SEQRES  38 C  504  TYR PHE PRO HIS ASN ASP ASP ALA LYS THR GLY ILE THR          
SEQRES  39 C  504  LEU SER GLY LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 E  504  ASN VAL GLU GLU GLU THR LYS TYR ILE GLU LEU MET ILE          
SEQRES   2 E  504  VAL ASN ASP HIS LEU MET PHE LYS LYS HIS ARG LEU SER          
SEQRES   3 E  504  VAL VAL HIS THR ASN THR TYR ALA LYS SER VAL VAL ASN          
SEQRES   4 E  504  MET ALA ASP LEU ILE TYR LYS ASP GLN LEU LYS THR ARG          
SEQRES   5 E  504  ILE VAL LEU VAL ALA MET GLU THR TRP ALA THR ASP ASN          
SEQRES   6 E  504  LYS PHE ALA ILE SER GLU ASN PRO LEU ILE THR LEU ARG          
SEQRES   7 E  504  GLU PHE MET LYS TYR ARG ARG ASP PHE ILE LYS GLU LYS          
SEQRES   8 E  504  SER ASP ALA VAL HIS LEU PHE SER GLY SER GLN PHE GLU          
SEQRES   9 E  504  SER SER ARG SER GLY ALA ALA TYR ILE GLY GLY ILE CYS          
SEQRES  10 E  504  SER LEU LEU LYS GLY GLY GLY VAL ASN GLU PHE GLY LYS          
SEQRES  11 E  504  THR ASP LEU MET ALA VAL THR LEU ALA GLN SER LEU ALA          
SEQRES  12 E  504  HIS ASN ILE GLY ILE ILE SER ASP LYS ARG LYS LEU ALA          
SEQRES  13 E  504  SER GLY GLU CYS LYS CYS GLU ASP THR TRP SER GLY CYS          
SEQRES  14 E  504  ILE MET GLY ASP THR GLY TYR TYR LEU PRO LYS LYS PHE          
SEQRES  15 E  504  THR GLN CYS ASN ILE GLU GLU TYR HIS ASP PHE LEU ASN          
SEQRES  16 E  504  SER GLY GLY GLY ALA CYS LEU PHE ASN LYS PRO SER LYS          
SEQRES  17 E  504  LEU LEU ASP PRO PRO GLU CYS GLY ASN GLY PHE ILE GLU          
SEQRES  18 E  504  THR GLY GLU GLU CYS ASP CYS GLY THR PRO ALA GLU CYS          
SEQRES  19 E  504  VAL LEU GLU GLY ALA GLU CYS CYS LYS LYS CYS THR LEU          
SEQRES  20 E  504  THR GLN ASP SER GLN CYS SER ASP GLY LEU CYS CYS LYS          
SEQRES  21 E  504  LYS CYS LYS PHE GLN PRO MET GLY THR VAL CYS ARG GLU          
SEQRES  22 E  504  ALA VAL ASN ASP CYS ASP ILE ARG GLU THR CYS SER GLY          
SEQRES  23 E  504  ASN SER SER GLN CYS ALA PRO ASN ILE HIS LYS MET ASP          
SEQRES  24 E  504  GLY TYR SER CYS ASP GLY VAL GLN GLY ILE CYS PHE GLY          
SEQRES  25 E  504  GLY ARG CYS LYS THR ARG ASP ARG GLN CYS LYS TYR ILE          
SEQRES  26 E  504  TRP GLY GLN LYS VAL THR ALA SER ASP LYS TYR CYS TYR          
SEQRES  27 E  504  GLU LYS LEU ASN ILE GLU GLY THR GLU LYS GLY ASN CYS          
SEQRES  28 E  504  GLY LYS ASP LYS ASP THR TRP ILE GLN CYS ASN LYS ARG          
SEQRES  29 E  504  ASP VAL LEU CYS GLY TYR LEU LEU CYS THR ASN ILE GLY          
SEQRES  30 E  504  ASN ILE PRO ARG LEU GLY GLU LEU ASP GLY GLU ILE THR          
SEQRES  31 E  504  SER THR LEU VAL VAL GLN GLN GLY ARG THR LEU ASN CYS          
SEQRES  32 E  504  SER GLY GLY HIS VAL LYS LEU GLU GLU ASP VAL ASP LEU          
SEQRES  33 E  504  GLY TYR VAL GLU ASP GLY THR PRO CYS GLY PRO GLN MET          
SEQRES  34 E  504  MET CYS LEU GLU HIS ARG CYS LEU PRO VAL ALA SER PHE          
SEQRES  35 E  504  ASN PHE SER THR CYS LEU SER SER LYS GLU GLY THR ILE          
SEQRES  36 E  504  CYS SER GLY ASN GLY VAL CYS SER ASN GLU LEU LYS CYS          
SEQRES  37 E  504  VAL CYS ASN ARG HIS TRP ILE GLY SER ASP CYS ASN THR          
SEQRES  38 E  504  TYR PHE PRO HIS ASN ASP ASP ALA LYS THR GLY ILE THR          
SEQRES  39 E  504  LEU SER GLY LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 G  504  ASN VAL GLU GLU GLU THR LYS TYR ILE GLU LEU MET ILE          
SEQRES   2 G  504  VAL ASN ASP HIS LEU MET PHE LYS LYS HIS ARG LEU SER          
SEQRES   3 G  504  VAL VAL HIS THR ASN THR TYR ALA LYS SER VAL VAL ASN          
SEQRES   4 G  504  MET ALA ASP LEU ILE TYR LYS ASP GLN LEU LYS THR ARG          
SEQRES   5 G  504  ILE VAL LEU VAL ALA MET GLU THR TRP ALA THR ASP ASN          
SEQRES   6 G  504  LYS PHE ALA ILE SER GLU ASN PRO LEU ILE THR LEU ARG          
SEQRES   7 G  504  GLU PHE MET LYS TYR ARG ARG ASP PHE ILE LYS GLU LYS          
SEQRES   8 G  504  SER ASP ALA VAL HIS LEU PHE SER GLY SER GLN PHE GLU          
SEQRES   9 G  504  SER SER ARG SER GLY ALA ALA TYR ILE GLY GLY ILE CYS          
SEQRES  10 G  504  SER LEU LEU LYS GLY GLY GLY VAL ASN GLU PHE GLY LYS          
SEQRES  11 G  504  THR ASP LEU MET ALA VAL THR LEU ALA GLN SER LEU ALA          
SEQRES  12 G  504  HIS ASN ILE GLY ILE ILE SER ASP LYS ARG LYS LEU ALA          
SEQRES  13 G  504  SER GLY GLU CYS LYS CYS GLU ASP THR TRP SER GLY CYS          
SEQRES  14 G  504  ILE MET GLY ASP THR GLY TYR TYR LEU PRO LYS LYS PHE          
SEQRES  15 G  504  THR GLN CYS ASN ILE GLU GLU TYR HIS ASP PHE LEU ASN          
SEQRES  16 G  504  SER GLY GLY GLY ALA CYS LEU PHE ASN LYS PRO SER LYS          
SEQRES  17 G  504  LEU LEU ASP PRO PRO GLU CYS GLY ASN GLY PHE ILE GLU          
SEQRES  18 G  504  THR GLY GLU GLU CYS ASP CYS GLY THR PRO ALA GLU CYS          
SEQRES  19 G  504  VAL LEU GLU GLY ALA GLU CYS CYS LYS LYS CYS THR LEU          
SEQRES  20 G  504  THR GLN ASP SER GLN CYS SER ASP GLY LEU CYS CYS LYS          
SEQRES  21 G  504  LYS CYS LYS PHE GLN PRO MET GLY THR VAL CYS ARG GLU          
SEQRES  22 G  504  ALA VAL ASN ASP CYS ASP ILE ARG GLU THR CYS SER GLY          
SEQRES  23 G  504  ASN SER SER GLN CYS ALA PRO ASN ILE HIS LYS MET ASP          
SEQRES  24 G  504  GLY TYR SER CYS ASP GLY VAL GLN GLY ILE CYS PHE GLY          
SEQRES  25 G  504  GLY ARG CYS LYS THR ARG ASP ARG GLN CYS LYS TYR ILE          
SEQRES  26 G  504  TRP GLY GLN LYS VAL THR ALA SER ASP LYS TYR CYS TYR          
SEQRES  27 G  504  GLU LYS LEU ASN ILE GLU GLY THR GLU LYS GLY ASN CYS          
SEQRES  28 G  504  GLY LYS ASP LYS ASP THR TRP ILE GLN CYS ASN LYS ARG          
SEQRES  29 G  504  ASP VAL LEU CYS GLY TYR LEU LEU CYS THR ASN ILE GLY          
SEQRES  30 G  504  ASN ILE PRO ARG LEU GLY GLU LEU ASP GLY GLU ILE THR          
SEQRES  31 G  504  SER THR LEU VAL VAL GLN GLN GLY ARG THR LEU ASN CYS          
SEQRES  32 G  504  SER GLY GLY HIS VAL LYS LEU GLU GLU ASP VAL ASP LEU          
SEQRES  33 G  504  GLY TYR VAL GLU ASP GLY THR PRO CYS GLY PRO GLN MET          
SEQRES  34 G  504  MET CYS LEU GLU HIS ARG CYS LEU PRO VAL ALA SER PHE          
SEQRES  35 G  504  ASN PHE SER THR CYS LEU SER SER LYS GLU GLY THR ILE          
SEQRES  36 G  504  CYS SER GLY ASN GLY VAL CYS SER ASN GLU LEU LYS CYS          
SEQRES  37 G  504  VAL CYS ASN ARG HIS TRP ILE GLY SER ASP CYS ASN THR          
SEQRES  38 G  504  TYR PHE PRO HIS ASN ASP ASP ALA LYS THR GLY ILE THR          
SEQRES  39 G  504  LEU SER GLY LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 I  504  ASN VAL GLU GLU GLU THR LYS TYR ILE GLU LEU MET ILE          
SEQRES   2 I  504  VAL ASN ASP HIS LEU MET PHE LYS LYS HIS ARG LEU SER          
SEQRES   3 I  504  VAL VAL HIS THR ASN THR TYR ALA LYS SER VAL VAL ASN          
SEQRES   4 I  504  MET ALA ASP LEU ILE TYR LYS ASP GLN LEU LYS THR ARG          
SEQRES   5 I  504  ILE VAL LEU VAL ALA MET GLU THR TRP ALA THR ASP ASN          
SEQRES   6 I  504  LYS PHE ALA ILE SER GLU ASN PRO LEU ILE THR LEU ARG          
SEQRES   7 I  504  GLU PHE MET LYS TYR ARG ARG ASP PHE ILE LYS GLU LYS          
SEQRES   8 I  504  SER ASP ALA VAL HIS LEU PHE SER GLY SER GLN PHE GLU          
SEQRES   9 I  504  SER SER ARG SER GLY ALA ALA TYR ILE GLY GLY ILE CYS          
SEQRES  10 I  504  SER LEU LEU LYS GLY GLY GLY VAL ASN GLU PHE GLY LYS          
SEQRES  11 I  504  THR ASP LEU MET ALA VAL THR LEU ALA GLN SER LEU ALA          
SEQRES  12 I  504  HIS ASN ILE GLY ILE ILE SER ASP LYS ARG LYS LEU ALA          
SEQRES  13 I  504  SER GLY GLU CYS LYS CYS GLU ASP THR TRP SER GLY CYS          
SEQRES  14 I  504  ILE MET GLY ASP THR GLY TYR TYR LEU PRO LYS LYS PHE          
SEQRES  15 I  504  THR GLN CYS ASN ILE GLU GLU TYR HIS ASP PHE LEU ASN          
SEQRES  16 I  504  SER GLY GLY GLY ALA CYS LEU PHE ASN LYS PRO SER LYS          
SEQRES  17 I  504  LEU LEU ASP PRO PRO GLU CYS GLY ASN GLY PHE ILE GLU          
SEQRES  18 I  504  THR GLY GLU GLU CYS ASP CYS GLY THR PRO ALA GLU CYS          
SEQRES  19 I  504  VAL LEU GLU GLY ALA GLU CYS CYS LYS LYS CYS THR LEU          
SEQRES  20 I  504  THR GLN ASP SER GLN CYS SER ASP GLY LEU CYS CYS LYS          
SEQRES  21 I  504  LYS CYS LYS PHE GLN PRO MET GLY THR VAL CYS ARG GLU          
SEQRES  22 I  504  ALA VAL ASN ASP CYS ASP ILE ARG GLU THR CYS SER GLY          
SEQRES  23 I  504  ASN SER SER GLN CYS ALA PRO ASN ILE HIS LYS MET ASP          
SEQRES  24 I  504  GLY TYR SER CYS ASP GLY VAL GLN GLY ILE CYS PHE GLY          
SEQRES  25 I  504  GLY ARG CYS LYS THR ARG ASP ARG GLN CYS LYS TYR ILE          
SEQRES  26 I  504  TRP GLY GLN LYS VAL THR ALA SER ASP LYS TYR CYS TYR          
SEQRES  27 I  504  GLU LYS LEU ASN ILE GLU GLY THR GLU LYS GLY ASN CYS          
SEQRES  28 I  504  GLY LYS ASP LYS ASP THR TRP ILE GLN CYS ASN LYS ARG          
SEQRES  29 I  504  ASP VAL LEU CYS GLY TYR LEU LEU CYS THR ASN ILE GLY          
SEQRES  30 I  504  ASN ILE PRO ARG LEU GLY GLU LEU ASP GLY GLU ILE THR          
SEQRES  31 I  504  SER THR LEU VAL VAL GLN GLN GLY ARG THR LEU ASN CYS          
SEQRES  32 I  504  SER GLY GLY HIS VAL LYS LEU GLU GLU ASP VAL ASP LEU          
SEQRES  33 I  504  GLY TYR VAL GLU ASP GLY THR PRO CYS GLY PRO GLN MET          
SEQRES  34 I  504  MET CYS LEU GLU HIS ARG CYS LEU PRO VAL ALA SER PHE          
SEQRES  35 I  504  ASN PHE SER THR CYS LEU SER SER LYS GLU GLY THR ILE          
SEQRES  36 I  504  CYS SER GLY ASN GLY VAL CYS SER ASN GLU LEU LYS CYS          
SEQRES  37 I  504  VAL CYS ASN ARG HIS TRP ILE GLY SER ASP CYS ASN THR          
SEQRES  38 I  504  TYR PHE PRO HIS ASN ASP ASP ALA LYS THR GLY ILE THR          
SEQRES  39 I  504  LEU SER GLY LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 K  504  ASN VAL GLU GLU GLU THR LYS TYR ILE GLU LEU MET ILE          
SEQRES   2 K  504  VAL ASN ASP HIS LEU MET PHE LYS LYS HIS ARG LEU SER          
SEQRES   3 K  504  VAL VAL HIS THR ASN THR TYR ALA LYS SER VAL VAL ASN          
SEQRES   4 K  504  MET ALA ASP LEU ILE TYR LYS ASP GLN LEU LYS THR ARG          
SEQRES   5 K  504  ILE VAL LEU VAL ALA MET GLU THR TRP ALA THR ASP ASN          
SEQRES   6 K  504  LYS PHE ALA ILE SER GLU ASN PRO LEU ILE THR LEU ARG          
SEQRES   7 K  504  GLU PHE MET LYS TYR ARG ARG ASP PHE ILE LYS GLU LYS          
SEQRES   8 K  504  SER ASP ALA VAL HIS LEU PHE SER GLY SER GLN PHE GLU          
SEQRES   9 K  504  SER SER ARG SER GLY ALA ALA TYR ILE GLY GLY ILE CYS          
SEQRES  10 K  504  SER LEU LEU LYS GLY GLY GLY VAL ASN GLU PHE GLY LYS          
SEQRES  11 K  504  THR ASP LEU MET ALA VAL THR LEU ALA GLN SER LEU ALA          
SEQRES  12 K  504  HIS ASN ILE GLY ILE ILE SER ASP LYS ARG LYS LEU ALA          
SEQRES  13 K  504  SER GLY GLU CYS LYS CYS GLU ASP THR TRP SER GLY CYS          
SEQRES  14 K  504  ILE MET GLY ASP THR GLY TYR TYR LEU PRO LYS LYS PHE          
SEQRES  15 K  504  THR GLN CYS ASN ILE GLU GLU TYR HIS ASP PHE LEU ASN          
SEQRES  16 K  504  SER GLY GLY GLY ALA CYS LEU PHE ASN LYS PRO SER LYS          
SEQRES  17 K  504  LEU LEU ASP PRO PRO GLU CYS GLY ASN GLY PHE ILE GLU          
SEQRES  18 K  504  THR GLY GLU GLU CYS ASP CYS GLY THR PRO ALA GLU CYS          
SEQRES  19 K  504  VAL LEU GLU GLY ALA GLU CYS CYS LYS LYS CYS THR LEU          
SEQRES  20 K  504  THR GLN ASP SER GLN CYS SER ASP GLY LEU CYS CYS LYS          
SEQRES  21 K  504  LYS CYS LYS PHE GLN PRO MET GLY THR VAL CYS ARG GLU          
SEQRES  22 K  504  ALA VAL ASN ASP CYS ASP ILE ARG GLU THR CYS SER GLY          
SEQRES  23 K  504  ASN SER SER GLN CYS ALA PRO ASN ILE HIS LYS MET ASP          
SEQRES  24 K  504  GLY TYR SER CYS ASP GLY VAL GLN GLY ILE CYS PHE GLY          
SEQRES  25 K  504  GLY ARG CYS LYS THR ARG ASP ARG GLN CYS LYS TYR ILE          
SEQRES  26 K  504  TRP GLY GLN LYS VAL THR ALA SER ASP LYS TYR CYS TYR          
SEQRES  27 K  504  GLU LYS LEU ASN ILE GLU GLY THR GLU LYS GLY ASN CYS          
SEQRES  28 K  504  GLY LYS ASP LYS ASP THR TRP ILE GLN CYS ASN LYS ARG          
SEQRES  29 K  504  ASP VAL LEU CYS GLY TYR LEU LEU CYS THR ASN ILE GLY          
SEQRES  30 K  504  ASN ILE PRO ARG LEU GLY GLU LEU ASP GLY GLU ILE THR          
SEQRES  31 K  504  SER THR LEU VAL VAL GLN GLN GLY ARG THR LEU ASN CYS          
SEQRES  32 K  504  SER GLY GLY HIS VAL LYS LEU GLU GLU ASP VAL ASP LEU          
SEQRES  33 K  504  GLY TYR VAL GLU ASP GLY THR PRO CYS GLY PRO GLN MET          
SEQRES  34 K  504  MET CYS LEU GLU HIS ARG CYS LEU PRO VAL ALA SER PHE          
SEQRES  35 K  504  ASN PHE SER THR CYS LEU SER SER LYS GLU GLY THR ILE          
SEQRES  36 K  504  CYS SER GLY ASN GLY VAL CYS SER ASN GLU LEU LYS CYS          
SEQRES  37 K  504  VAL CYS ASN ARG HIS TRP ILE GLY SER ASP CYS ASN THR          
SEQRES  38 K  504  TYR PHE PRO HIS ASN ASP ASP ALA LYS THR GLY ILE THR          
SEQRES  39 K  504  LEU SER GLY LYS HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  347  ASP ALA ALA GLN PRO ALA THR GLU PHE ALA LYS SER GLN          
SEQRES   2 B  347  ASP LEU PRO TYR GLN SER LEU SER ILE ASP THR PHE SER          
SEQRES   3 B  347  TYR LEU ASN ASP GLU TYR VAL VAL ILE ALA GLN PRO PHE          
SEQRES   4 B  347  THR GLY LYS CYS ILE PHE LEU GLU TRP ASP HIS VAL GLU          
SEQRES   5 B  347  LYS THR PHE ARG ASN TYR ASP ASN ILE THR GLY THR SER          
SEQRES   6 B  347  THR VAL VAL CYS LYS PRO ILE VAL ILE GLU THR GLN LEU          
SEQRES   7 B  347  TYR VAL ILE VAL ALA GLN LEU PHE GLY GLY SER HIS ILE          
SEQRES   8 B  347  TYR LYS ARG ASP SER PHE ALA ASN LYS PHE ILE LYS ILE          
SEQRES   9 B  347  GLN ASP ILE GLU ILE LEU LYS ILE ARG LYS PRO ASN ASP          
SEQRES  10 B  347  ILE GLU THR PHE LYS ILE GLU ASN ASN TRP TYR PHE VAL          
SEQRES  11 B  347  VAL ALA ASP SER SER LYS ALA GLY PHE THR THR ILE TYR          
SEQRES  12 B  347  LYS TRP ASN GLY ASN GLY PHE TYR SER HIS GLN SER LEU          
SEQRES  13 B  347  HIS ALA TRP TYR ARG ASP THR ASP VAL GLU TYR LEU GLU          
SEQRES  14 B  347  ILE VAL ARG THR PRO GLN THR LEU ARG THR PRO HIS LEU          
SEQRES  15 B  347  ILE LEU SER SER SER SER GLN ARG PRO VAL ILE TYR GLN          
SEQRES  16 B  347  TRP ASN LYS ALA THR GLN LEU PHE THR ASN GLN THR ASP          
SEQRES  17 B  347  ILE PRO ASN MET GLU ASP VAL TYR ALA VAL LYS HIS PHE          
SEQRES  18 B  347  SER VAL LYS GLY ASP VAL TYR ILE CYS LEU THR ARG PHE          
SEQRES  19 B  347  ILE GLY ASP SER LYS VAL MET LYS TRP GLY GLY SER SER          
SEQRES  20 B  347  PHE GLN ASP ILE GLN ARG MET PRO SER ARG GLY SER MET          
SEQRES  21 B  347  VAL PHE GLN PRO LEU GLN ILE ASN ASN TYR GLN TYR ALA          
SEQRES  22 B  347  ILE LEU GLY SER ASP TYR SER PHE THR GLN VAL TYR ASN          
SEQRES  23 B  347  TRP ASP ALA GLU LYS ALA LYS PHE VAL LYS PHE GLN GLU          
SEQRES  24 B  347  LEU ASN VAL GLN ALA PRO ARG SER PHE THR HIS VAL SER          
SEQRES  25 B  347  ILE ASN LYS ARG ASN PHE LEU PHE ALA SER SER PHE LYS          
SEQRES  26 B  347  GLY ASN THR GLN ILE TYR LYS HIS VAL ILE VAL ASP LEU          
SEQRES  27 B  347  SER ALA LYS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 D  347  ASP ALA ALA GLN PRO ALA THR GLU PHE ALA LYS SER GLN          
SEQRES   2 D  347  ASP LEU PRO TYR GLN SER LEU SER ILE ASP THR PHE SER          
SEQRES   3 D  347  TYR LEU ASN ASP GLU TYR VAL VAL ILE ALA GLN PRO PHE          
SEQRES   4 D  347  THR GLY LYS CYS ILE PHE LEU GLU TRP ASP HIS VAL GLU          
SEQRES   5 D  347  LYS THR PHE ARG ASN TYR ASP ASN ILE THR GLY THR SER          
SEQRES   6 D  347  THR VAL VAL CYS LYS PRO ILE VAL ILE GLU THR GLN LEU          
SEQRES   7 D  347  TYR VAL ILE VAL ALA GLN LEU PHE GLY GLY SER HIS ILE          
SEQRES   8 D  347  TYR LYS ARG ASP SER PHE ALA ASN LYS PHE ILE LYS ILE          
SEQRES   9 D  347  GLN ASP ILE GLU ILE LEU LYS ILE ARG LYS PRO ASN ASP          
SEQRES  10 D  347  ILE GLU THR PHE LYS ILE GLU ASN ASN TRP TYR PHE VAL          
SEQRES  11 D  347  VAL ALA ASP SER SER LYS ALA GLY PHE THR THR ILE TYR          
SEQRES  12 D  347  LYS TRP ASN GLY ASN GLY PHE TYR SER HIS GLN SER LEU          
SEQRES  13 D  347  HIS ALA TRP TYR ARG ASP THR ASP VAL GLU TYR LEU GLU          
SEQRES  14 D  347  ILE VAL ARG THR PRO GLN THR LEU ARG THR PRO HIS LEU          
SEQRES  15 D  347  ILE LEU SER SER SER SER GLN ARG PRO VAL ILE TYR GLN          
SEQRES  16 D  347  TRP ASN LYS ALA THR GLN LEU PHE THR ASN GLN THR ASP          
SEQRES  17 D  347  ILE PRO ASN MET GLU ASP VAL TYR ALA VAL LYS HIS PHE          
SEQRES  18 D  347  SER VAL LYS GLY ASP VAL TYR ILE CYS LEU THR ARG PHE          
SEQRES  19 D  347  ILE GLY ASP SER LYS VAL MET LYS TRP GLY GLY SER SER          
SEQRES  20 D  347  PHE GLN ASP ILE GLN ARG MET PRO SER ARG GLY SER MET          
SEQRES  21 D  347  VAL PHE GLN PRO LEU GLN ILE ASN ASN TYR GLN TYR ALA          
SEQRES  22 D  347  ILE LEU GLY SER ASP TYR SER PHE THR GLN VAL TYR ASN          
SEQRES  23 D  347  TRP ASP ALA GLU LYS ALA LYS PHE VAL LYS PHE GLN GLU          
SEQRES  24 D  347  LEU ASN VAL GLN ALA PRO ARG SER PHE THR HIS VAL SER          
SEQRES  25 D  347  ILE ASN LYS ARG ASN PHE LEU PHE ALA SER SER PHE LYS          
SEQRES  26 D  347  GLY ASN THR GLN ILE TYR LYS HIS VAL ILE VAL ASP LEU          
SEQRES  27 D  347  SER ALA LYS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 F  347  ASP ALA ALA GLN PRO ALA THR GLU PHE ALA LYS SER GLN          
SEQRES   2 F  347  ASP LEU PRO TYR GLN SER LEU SER ILE ASP THR PHE SER          
SEQRES   3 F  347  TYR LEU ASN ASP GLU TYR VAL VAL ILE ALA GLN PRO PHE          
SEQRES   4 F  347  THR GLY LYS CYS ILE PHE LEU GLU TRP ASP HIS VAL GLU          
SEQRES   5 F  347  LYS THR PHE ARG ASN TYR ASP ASN ILE THR GLY THR SER          
SEQRES   6 F  347  THR VAL VAL CYS LYS PRO ILE VAL ILE GLU THR GLN LEU          
SEQRES   7 F  347  TYR VAL ILE VAL ALA GLN LEU PHE GLY GLY SER HIS ILE          
SEQRES   8 F  347  TYR LYS ARG ASP SER PHE ALA ASN LYS PHE ILE LYS ILE          
SEQRES   9 F  347  GLN ASP ILE GLU ILE LEU LYS ILE ARG LYS PRO ASN ASP          
SEQRES  10 F  347  ILE GLU THR PHE LYS ILE GLU ASN ASN TRP TYR PHE VAL          
SEQRES  11 F  347  VAL ALA ASP SER SER LYS ALA GLY PHE THR THR ILE TYR          
SEQRES  12 F  347  LYS TRP ASN GLY ASN GLY PHE TYR SER HIS GLN SER LEU          
SEQRES  13 F  347  HIS ALA TRP TYR ARG ASP THR ASP VAL GLU TYR LEU GLU          
SEQRES  14 F  347  ILE VAL ARG THR PRO GLN THR LEU ARG THR PRO HIS LEU          
SEQRES  15 F  347  ILE LEU SER SER SER SER GLN ARG PRO VAL ILE TYR GLN          
SEQRES  16 F  347  TRP ASN LYS ALA THR GLN LEU PHE THR ASN GLN THR ASP          
SEQRES  17 F  347  ILE PRO ASN MET GLU ASP VAL TYR ALA VAL LYS HIS PHE          
SEQRES  18 F  347  SER VAL LYS GLY ASP VAL TYR ILE CYS LEU THR ARG PHE          
SEQRES  19 F  347  ILE GLY ASP SER LYS VAL MET LYS TRP GLY GLY SER SER          
SEQRES  20 F  347  PHE GLN ASP ILE GLN ARG MET PRO SER ARG GLY SER MET          
SEQRES  21 F  347  VAL PHE GLN PRO LEU GLN ILE ASN ASN TYR GLN TYR ALA          
SEQRES  22 F  347  ILE LEU GLY SER ASP TYR SER PHE THR GLN VAL TYR ASN          
SEQRES  23 F  347  TRP ASP ALA GLU LYS ALA LYS PHE VAL LYS PHE GLN GLU          
SEQRES  24 F  347  LEU ASN VAL GLN ALA PRO ARG SER PHE THR HIS VAL SER          
SEQRES  25 F  347  ILE ASN LYS ARG ASN PHE LEU PHE ALA SER SER PHE LYS          
SEQRES  26 F  347  GLY ASN THR GLN ILE TYR LYS HIS VAL ILE VAL ASP LEU          
SEQRES  27 F  347  SER ALA LYS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 H  347  ASP ALA ALA GLN PRO ALA THR GLU PHE ALA LYS SER GLN          
SEQRES   2 H  347  ASP LEU PRO TYR GLN SER LEU SER ILE ASP THR PHE SER          
SEQRES   3 H  347  TYR LEU ASN ASP GLU TYR VAL VAL ILE ALA GLN PRO PHE          
SEQRES   4 H  347  THR GLY LYS CYS ILE PHE LEU GLU TRP ASP HIS VAL GLU          
SEQRES   5 H  347  LYS THR PHE ARG ASN TYR ASP ASN ILE THR GLY THR SER          
SEQRES   6 H  347  THR VAL VAL CYS LYS PRO ILE VAL ILE GLU THR GLN LEU          
SEQRES   7 H  347  TYR VAL ILE VAL ALA GLN LEU PHE GLY GLY SER HIS ILE          
SEQRES   8 H  347  TYR LYS ARG ASP SER PHE ALA ASN LYS PHE ILE LYS ILE          
SEQRES   9 H  347  GLN ASP ILE GLU ILE LEU LYS ILE ARG LYS PRO ASN ASP          
SEQRES  10 H  347  ILE GLU THR PHE LYS ILE GLU ASN ASN TRP TYR PHE VAL          
SEQRES  11 H  347  VAL ALA ASP SER SER LYS ALA GLY PHE THR THR ILE TYR          
SEQRES  12 H  347  LYS TRP ASN GLY ASN GLY PHE TYR SER HIS GLN SER LEU          
SEQRES  13 H  347  HIS ALA TRP TYR ARG ASP THR ASP VAL GLU TYR LEU GLU          
SEQRES  14 H  347  ILE VAL ARG THR PRO GLN THR LEU ARG THR PRO HIS LEU          
SEQRES  15 H  347  ILE LEU SER SER SER SER GLN ARG PRO VAL ILE TYR GLN          
SEQRES  16 H  347  TRP ASN LYS ALA THR GLN LEU PHE THR ASN GLN THR ASP          
SEQRES  17 H  347  ILE PRO ASN MET GLU ASP VAL TYR ALA VAL LYS HIS PHE          
SEQRES  18 H  347  SER VAL LYS GLY ASP VAL TYR ILE CYS LEU THR ARG PHE          
SEQRES  19 H  347  ILE GLY ASP SER LYS VAL MET LYS TRP GLY GLY SER SER          
SEQRES  20 H  347  PHE GLN ASP ILE GLN ARG MET PRO SER ARG GLY SER MET          
SEQRES  21 H  347  VAL PHE GLN PRO LEU GLN ILE ASN ASN TYR GLN TYR ALA          
SEQRES  22 H  347  ILE LEU GLY SER ASP TYR SER PHE THR GLN VAL TYR ASN          
SEQRES  23 H  347  TRP ASP ALA GLU LYS ALA LYS PHE VAL LYS PHE GLN GLU          
SEQRES  24 H  347  LEU ASN VAL GLN ALA PRO ARG SER PHE THR HIS VAL SER          
SEQRES  25 H  347  ILE ASN LYS ARG ASN PHE LEU PHE ALA SER SER PHE LYS          
SEQRES  26 H  347  GLY ASN THR GLN ILE TYR LYS HIS VAL ILE VAL ASP LEU          
SEQRES  27 H  347  SER ALA LYS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 J  347  ASP ALA ALA GLN PRO ALA THR GLU PHE ALA LYS SER GLN          
SEQRES   2 J  347  ASP LEU PRO TYR GLN SER LEU SER ILE ASP THR PHE SER          
SEQRES   3 J  347  TYR LEU ASN ASP GLU TYR VAL VAL ILE ALA GLN PRO PHE          
SEQRES   4 J  347  THR GLY LYS CYS ILE PHE LEU GLU TRP ASP HIS VAL GLU          
SEQRES   5 J  347  LYS THR PHE ARG ASN TYR ASP ASN ILE THR GLY THR SER          
SEQRES   6 J  347  THR VAL VAL CYS LYS PRO ILE VAL ILE GLU THR GLN LEU          
SEQRES   7 J  347  TYR VAL ILE VAL ALA GLN LEU PHE GLY GLY SER HIS ILE          
SEQRES   8 J  347  TYR LYS ARG ASP SER PHE ALA ASN LYS PHE ILE LYS ILE          
SEQRES   9 J  347  GLN ASP ILE GLU ILE LEU LYS ILE ARG LYS PRO ASN ASP          
SEQRES  10 J  347  ILE GLU THR PHE LYS ILE GLU ASN ASN TRP TYR PHE VAL          
SEQRES  11 J  347  VAL ALA ASP SER SER LYS ALA GLY PHE THR THR ILE TYR          
SEQRES  12 J  347  LYS TRP ASN GLY ASN GLY PHE TYR SER HIS GLN SER LEU          
SEQRES  13 J  347  HIS ALA TRP TYR ARG ASP THR ASP VAL GLU TYR LEU GLU          
SEQRES  14 J  347  ILE VAL ARG THR PRO GLN THR LEU ARG THR PRO HIS LEU          
SEQRES  15 J  347  ILE LEU SER SER SER SER GLN ARG PRO VAL ILE TYR GLN          
SEQRES  16 J  347  TRP ASN LYS ALA THR GLN LEU PHE THR ASN GLN THR ASP          
SEQRES  17 J  347  ILE PRO ASN MET GLU ASP VAL TYR ALA VAL LYS HIS PHE          
SEQRES  18 J  347  SER VAL LYS GLY ASP VAL TYR ILE CYS LEU THR ARG PHE          
SEQRES  19 J  347  ILE GLY ASP SER LYS VAL MET LYS TRP GLY GLY SER SER          
SEQRES  20 J  347  PHE GLN ASP ILE GLN ARG MET PRO SER ARG GLY SER MET          
SEQRES  21 J  347  VAL PHE GLN PRO LEU GLN ILE ASN ASN TYR GLN TYR ALA          
SEQRES  22 J  347  ILE LEU GLY SER ASP TYR SER PHE THR GLN VAL TYR ASN          
SEQRES  23 J  347  TRP ASP ALA GLU LYS ALA LYS PHE VAL LYS PHE GLN GLU          
SEQRES  24 J  347  LEU ASN VAL GLN ALA PRO ARG SER PHE THR HIS VAL SER          
SEQRES  25 J  347  ILE ASN LYS ARG ASN PHE LEU PHE ALA SER SER PHE LYS          
SEQRES  26 J  347  GLY ASN THR GLN ILE TYR LYS HIS VAL ILE VAL ASP LEU          
SEQRES  27 J  347  SER ALA LYS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 L  347  ASP ALA ALA GLN PRO ALA THR GLU PHE ALA LYS SER GLN          
SEQRES   2 L  347  ASP LEU PRO TYR GLN SER LEU SER ILE ASP THR PHE SER          
SEQRES   3 L  347  TYR LEU ASN ASP GLU TYR VAL VAL ILE ALA GLN PRO PHE          
SEQRES   4 L  347  THR GLY LYS CYS ILE PHE LEU GLU TRP ASP HIS VAL GLU          
SEQRES   5 L  347  LYS THR PHE ARG ASN TYR ASP ASN ILE THR GLY THR SER          
SEQRES   6 L  347  THR VAL VAL CYS LYS PRO ILE VAL ILE GLU THR GLN LEU          
SEQRES   7 L  347  TYR VAL ILE VAL ALA GLN LEU PHE GLY GLY SER HIS ILE          
SEQRES   8 L  347  TYR LYS ARG ASP SER PHE ALA ASN LYS PHE ILE LYS ILE          
SEQRES   9 L  347  GLN ASP ILE GLU ILE LEU LYS ILE ARG LYS PRO ASN ASP          
SEQRES  10 L  347  ILE GLU THR PHE LYS ILE GLU ASN ASN TRP TYR PHE VAL          
SEQRES  11 L  347  VAL ALA ASP SER SER LYS ALA GLY PHE THR THR ILE TYR          
SEQRES  12 L  347  LYS TRP ASN GLY ASN GLY PHE TYR SER HIS GLN SER LEU          
SEQRES  13 L  347  HIS ALA TRP TYR ARG ASP THR ASP VAL GLU TYR LEU GLU          
SEQRES  14 L  347  ILE VAL ARG THR PRO GLN THR LEU ARG THR PRO HIS LEU          
SEQRES  15 L  347  ILE LEU SER SER SER SER GLN ARG PRO VAL ILE TYR GLN          
SEQRES  16 L  347  TRP ASN LYS ALA THR GLN LEU PHE THR ASN GLN THR ASP          
SEQRES  17 L  347  ILE PRO ASN MET GLU ASP VAL TYR ALA VAL LYS HIS PHE          
SEQRES  18 L  347  SER VAL LYS GLY ASP VAL TYR ILE CYS LEU THR ARG PHE          
SEQRES  19 L  347  ILE GLY ASP SER LYS VAL MET LYS TRP GLY GLY SER SER          
SEQRES  20 L  347  PHE GLN ASP ILE GLN ARG MET PRO SER ARG GLY SER MET          
SEQRES  21 L  347  VAL PHE GLN PRO LEU GLN ILE ASN ASN TYR GLN TYR ALA          
SEQRES  22 L  347  ILE LEU GLY SER ASP TYR SER PHE THR GLN VAL TYR ASN          
SEQRES  23 L  347  TRP ASP ALA GLU LYS ALA LYS PHE VAL LYS PHE GLN GLU          
SEQRES  24 L  347  LEU ASN VAL GLN ALA PRO ARG SER PHE THR HIS VAL SER          
SEQRES  25 L  347  ILE ASN LYS ARG ASN PHE LEU PHE ALA SER SER PHE LYS          
SEQRES  26 L  347  GLY ASN THR GLN ILE TYR LYS HIS VAL ILE VAL ASP LEU          
SEQRES  27 L  347  SER ALA LYS HIS HIS HIS HIS HIS HIS                          
HET     CA  A 801       1                                                       
HET     CA  A 802       1                                                       
HET     CA  A 803       1                                                       
HET     CA  C 801       1                                                       
HET     CA  C 802       1                                                       
HET     CA  C 803       1                                                       
HET     CA  E 801       1                                                       
HET     CA  E 802       1                                                       
HET     CA  E 803       1                                                       
HET     CA  G 801       1                                                       
HET     CA  G 802       1                                                       
HET     CA  G 803       1                                                       
HET     CA  I 801       1                                                       
HET     CA  I 802       1                                                       
HET     CA  I 803       1                                                       
HET     CA  K 801       1                                                       
HET     CA  K 802       1                                                       
HET     CA  K 803       1                                                       
HET     CA  B 601       1                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    FUC  B 604      10                                                       
HET    NAG  B 605      14                                                       
HET    NAG  B 606      14                                                       
HET    BMA  B 607      11                                                       
HET     CA  D 601       1                                                       
HET    NAG  D 602      14                                                       
HET    NAG  D 603      14                                                       
HET    FUC  D 604      10                                                       
HET    NAG  D 605      14                                                       
HET    NAG  D 606      14                                                       
HET     CA  F 601       1                                                       
HET    NAG  F 602      14                                                       
HET    NAG  F 603      14                                                       
HET    FUC  F 604      10                                                       
HET    NAG  F 605      14                                                       
HET     CA  H 601       1                                                       
HET    NAG  H 602      14                                                       
HET    FUC  H 603      10                                                       
HET    NAG  H 604      14                                                       
HET    NAG  H 605      14                                                       
HET    BMA  H 606      11                                                       
HET     CA  J 601       1                                                       
HET    NAG  J 602      14                                                       
HET    NAG  J 603      14                                                       
HET    FUC  J 604      10                                                       
HET    NAG  J 605      14                                                       
HET    NAG  J 606      14                                                       
HET     CA  L 601       1                                                       
HET    NAG  L 602      14                                                       
HET    FUC  L 603      10                                                       
HET    NAG  L 604      14                                                       
HET    NAG  L 605      14                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
FORMUL  13   CA    24(CA 2+)                                                    
FORMUL  32  NAG    21(C8 H15 N O6)                                              
FORMUL  33  FUC    6(C6 H12 O5)                                                 
FORMUL  33  BMA    2(C6 H12 O6)                                                 
FORMUL  49  HOH   *914(H2 O)                                                    
HELIX    1 AA1 ASP A  248  HIS A  255  1                                   8    
HELIX    2 AA2 SER A  258  LEU A  281  1                                  24    
HELIX    3 AA3 ASN A  304  PHE A  319  1                                  16    
HELIX    4 AA4 LYS A  362  ILE A  378  1                                  17    
HELIX    5 AA5 ASP A  383  SER A  389  1                                   7    
HELIX    6 AA6 THR A  415  SER A  428  1                                  14    
HELIX    7 AA7 GLY A  431  PHE A  435  5                                   5    
HELIX    8 AA8 THR A  549  GLY A  559  1                                  11    
HELIX    9 AA9 ASP A  566  GLY A  577  1                                  12    
HELIX   10 AB1 ALA A  672  ASN A  675  5                                   4    
HELIX   11 AB2 THR A  686  GLY A  690  5                                   5    
HELIX   12 AB3 ASP C  248  HIS C  255  1                                   8    
HELIX   13 AB4 SER C  258  LEU C  281  1                                  24    
HELIX   14 AB5 ASN C  304  ILE C  320  1                                  17    
HELIX   15 AB6 LYS C  362  GLY C  379  1                                  18    
HELIX   16 AB7 ASP C  383  SER C  389  1                                   7    
HELIX   17 AB8 THR C  415  SER C  428  1                                  14    
HELIX   18 AB9 GLY C  431  PHE C  435  5                                   5    
HELIX   19 AC1 THR C  462  GLU C  469  1                                   8    
HELIX   20 AC2 THR C  549  GLY C  559  1                                  11    
HELIX   21 AC3 ASP C  566  ASN C  574  1                                   9    
HELIX   22 AC4 ASP C  597  GLY C  601  5                                   5    
HELIX   23 AC5 ALA C  672  ASN C  675  5                                   4    
HELIX   24 AC6 THR C  686  GLY C  690  5                                   5    
HELIX   25 AC7 ASP E  248  HIS E  255  1                                   8    
HELIX   26 AC8 SER E  258  LEU E  281  1                                  24    
HELIX   27 AC9 ASN E  304  PHE E  319  1                                  16    
HELIX   28 AD1 LYS E  362  GLY E  379  1                                  18    
HELIX   29 AD2 ASP E  383  SER E  389  1                                   7    
HELIX   30 AD3 THR E  415  SER E  428  1                                  14    
HELIX   31 AD4 GLY E  431  PHE E  435  5                                   5    
HELIX   32 AD5 THR E  462  VAL E  467  1                                   6    
HELIX   33 AD6 THR E  549  GLY E  559  1                                  11    
HELIX   34 AD7 ASP E  566  ASN E  574  1                                   9    
HELIX   35 AD8 ALA E  672  ASN E  675  5                                   4    
HELIX   36 AD9 THR E  686  GLY E  690  5                                   5    
HELIX   37 AE1 ASP G  248  HIS G  255  1                                   8    
HELIX   38 AE2 SER G  258  LEU G  281  1                                  24    
HELIX   39 AE3 ASN G  304  PHE G  319  1                                  16    
HELIX   40 AE4 LYS G  362  GLY G  379  1                                  18    
HELIX   41 AE5 ASP G  383  SER G  389  1                                   7    
HELIX   42 AE6 THR G  415  SER G  428  1                                  14    
HELIX   43 AE7 GLY G  431  PHE G  435  5                                   5    
HELIX   44 AE8 THR G  462  VAL G  467  1                                   6    
HELIX   45 AE9 THR G  549  GLY G  559  1                                  11    
HELIX   46 AF1 ASP G  566  ASN G  574  1                                   9    
HELIX   47 AF2 ARG G  596  GLY G  601  5                                   6    
HELIX   48 AF3 ALA G  672  ASN G  675  5                                   4    
HELIX   49 AF4 THR G  686  GLY G  690  5                                   5    
HELIX   50 AF5 ASP I  248  HIS I  255  1                                   8    
HELIX   51 AF6 SER I  258  LEU I  281  1                                  24    
HELIX   52 AF7 ASN I  304  ILE I  320  1                                  17    
HELIX   53 AF8 LYS I  362  ILE I  378  1                                  17    
HELIX   54 AF9 ASP I  383  SER I  389  1                                   7    
HELIX   55 AG1 THR I  415  SER I  428  1                                  14    
HELIX   56 AG2 GLY I  431  PHE I  435  5                                   5    
HELIX   57 AG3 THR I  462  VAL I  467  1                                   6    
HELIX   58 AG4 THR I  549  GLY I  559  1                                  11    
HELIX   59 AG5 ASP I  566  GLY I  577  1                                  12    
HELIX   60 AG6 ASP I  597  GLY I  601  5                                   5    
HELIX   61 AG7 ALA I  672  ASN I  675  5                                   4    
HELIX   62 AG8 THR I  686  GLY I  690  5                                   5    
HELIX   63 AG9 ASP K  248  HIS K  255  1                                   8    
HELIX   64 AH1 SER K  258  LEU K  281  1                                  24    
HELIX   65 AH2 ASN K  304  PHE K  319  1                                  16    
HELIX   66 AH3 LYS K  362  GLY K  379  1                                  18    
HELIX   67 AH4 ASP K  383  SER K  389  1                                   7    
HELIX   68 AH5 THR K  415  SER K  428  1                                  14    
HELIX   69 AH6 GLY K  431  PHE K  435  5                                   5    
HELIX   70 AH7 THR K  462  VAL K  467  1                                   6    
HELIX   71 AH8 THR K  549  GLY K  559  1                                  11    
HELIX   72 AH9 ASP K  566  ASN K  574  1                                   9    
HELIX   73 AI1 ALA K  672  ASN K  675  5                                   4    
HELIX   74 AI2 THR K  686  GLY K  690  5                                   5    
SHEET    1 AA1 5 THR A 283  THR A 292  0                                        
SHEET    2 AA1 5 LYS A 239  ASN A 247  1  N  ILE A 241   O  ARG A 284           
SHEET    3 AA1 5 ALA A 326  SER A 331  1  O  PHE A 330   N  VAL A 246           
SHEET    4 AA1 5 GLY A 355  GLU A 359  1  O  ASN A 358   N  LEU A 329           
SHEET    5 AA1 5 GLY A 341  ALA A 343 -1  N  ALA A 342   O  VAL A 357           
SHEET    1 AA2 2 CYS A 491  LYS A 492  0                                        
SHEET    2 AA2 2 LYS A 495  PHE A 496 -1  O  LYS A 495   N  LYS A 492           
SHEET    1 AA3 2 VAL A 502  ARG A 504  0                                        
SHEET    2 AA3 2 GLU A 514  THR A 515 -1  O  GLU A 514   N  ARG A 504           
SHEET    1 AA4 3 SER A 534  CYS A 535  0                                        
SHEET    2 AA4 3 GLY A 540  PHE A 543 -1  O  GLY A 540   N  CYS A 535           
SHEET    3 AA4 3 ARG A 546  LYS A 548 -1  O  ARG A 546   N  PHE A 543           
SHEET    1 AA5 2 THR A 563  ALA A 564  0                                        
SHEET    2 AA5 2 CYS A 605  THR A 606 -1  O  THR A 606   N  THR A 563           
SHEET    1 AA6 2 LYS A 585  ASP A 586  0                                        
SHEET    2 AA6 2 THR A 589  TRP A 590 -1  O  THR A 589   N  ASP A 586           
SHEET    1 AA7 3 GLU A 616  LEU A 617  0                                        
SHEET    2 AA7 3 VAL A 640  LYS A 641 -1  O  LYS A 641   N  GLU A 616           
SHEET    3 AA7 3 ASP A 647  LEU A 648 -1  O  LEU A 648   N  VAL A 640           
SHEET    1 AA8 2 THR A 622  THR A 624  0                                        
SHEET    2 AA8 2 CYS A 635  GLY A 637 -1  O  CYS A 635   N  THR A 624           
SHEET    1 AA9 3 PRO A 656  GLY A 658  0                                        
SHEET    2 AA9 3 MET A 661  CYS A 663 -1  O  MET A 661   N  GLY A 658           
SHEET    3 AA9 3 CYS A 668  PRO A 670 -1  O  LEU A 669   N  MET A 662           
SHEET    1 AB1 2 GLY A 692  CYS A 694  0                                        
SHEET    2 AB1 2 CYS A 700  CYS A 702 -1  O  VAL A 701   N  VAL A 693           
SHEET    1 AB2 2 TRP A 706  ILE A 707  0                                        
SHEET    2 AB2 2 THR A 713  TYR A 714 -1  O  THR A 713   N  ILE A 707           
SHEET    1 AB3 5 THR C 283  THR C 292  0                                        
SHEET    2 AB3 5 LYS C 239  ASN C 247  1  N  ILE C 241   O  ARG C 284           
SHEET    3 AB3 5 ALA C 326  SER C 331  1  O  PHE C 330   N  VAL C 246           
SHEET    4 AB3 5 GLY C 355  GLU C 359  1  O  ASN C 358   N  SER C 331           
SHEET    5 AB3 5 GLY C 341  ALA C 343 -1  N  ALA C 342   O  VAL C 357           
SHEET    1 AB4 2 CYS C 491  LYS C 492  0                                        
SHEET    2 AB4 2 LYS C 495  PHE C 496 -1  O  LYS C 495   N  LYS C 492           
SHEET    1 AB5 2 VAL C 502  ARG C 504  0                                        
SHEET    2 AB5 2 GLU C 514  THR C 515 -1  O  GLU C 514   N  ARG C 504           
SHEET    1 AB6 3 SER C 534  CYS C 535  0                                        
SHEET    2 AB6 3 GLY C 540  PHE C 543 -1  O  GLY C 540   N  CYS C 535           
SHEET    3 AB6 3 ARG C 546  LYS C 548 -1  O  ARG C 546   N  PHE C 543           
SHEET    1 AB7 2 THR C 563  ALA C 564  0                                        
SHEET    2 AB7 2 CYS C 605  THR C 606 -1  O  THR C 606   N  THR C 563           
SHEET    1 AB8 3 GLU C 616  LEU C 617  0                                        
SHEET    2 AB8 3 VAL C 640  LYS C 641 -1  O  LYS C 641   N  GLU C 616           
SHEET    3 AB8 3 ASP C 647  LEU C 648 -1  O  LEU C 648   N  VAL C 640           
SHEET    1 AB9 2 THR C 622  VAL C 626  0                                        
SHEET    2 AB9 2 LEU C 633  GLY C 637 -1  O  CYS C 635   N  THR C 624           
SHEET    1 AC1 3 PRO C 656  GLY C 658  0                                        
SHEET    2 AC1 3 MET C 661  CYS C 663 -1  O  MET C 661   N  CYS C 657           
SHEET    3 AC1 3 CYS C 668  PRO C 670 -1  O  LEU C 669   N  MET C 662           
SHEET    1 AC2 2 GLY C 692  CYS C 694  0                                        
SHEET    2 AC2 2 CYS C 700  CYS C 702 -1  O  VAL C 701   N  VAL C 693           
SHEET    1 AC3 2 TRP C 706  ILE C 707  0                                        
SHEET    2 AC3 2 THR C 713  TYR C 714 -1  O  THR C 713   N  ILE C 707           
SHEET    1 AC4 5 THR E 283  THR E 292  0                                        
SHEET    2 AC4 5 LYS E 239  ASN E 247  1  N  ILE E 241   O  ARG E 284           
SHEET    3 AC4 5 ALA E 326  SER E 331  1  O  PHE E 330   N  VAL E 246           
SHEET    4 AC4 5 GLY E 355  GLU E 359  1  O  ASN E 358   N  SER E 331           
SHEET    5 AC4 5 GLY E 341  ALA E 343 -1  N  ALA E 342   O  VAL E 357           
SHEET    1 AC5 2 CYS E 474  LYS E 475  0                                        
SHEET    2 AC5 2 THR E 478  LEU E 479 -1  O  THR E 478   N  LYS E 475           
SHEET    1 AC6 2 CYS E 491  LYS E 492  0                                        
SHEET    2 AC6 2 LYS E 495  PHE E 496 -1  O  LYS E 495   N  LYS E 492           
SHEET    1 AC7 2 VAL E 502  ARG E 504  0                                        
SHEET    2 AC7 2 GLU E 514  THR E 515 -1  O  GLU E 514   N  ARG E 504           
SHEET    1 AC8 3 SER E 534  CYS E 535  0                                        
SHEET    2 AC8 3 GLY E 540  PHE E 543 -1  O  GLY E 540   N  CYS E 535           
SHEET    3 AC8 3 ARG E 546  LYS E 548 -1  O  ARG E 546   N  PHE E 543           
SHEET    1 AC9 2 THR E 563  ALA E 564  0                                        
SHEET    2 AC9 2 CYS E 605  THR E 606 -1  O  THR E 606   N  THR E 563           
SHEET    1 AD1 3 GLU E 616  LEU E 617  0                                        
SHEET    2 AD1 3 VAL E 640  LYS E 641 -1  O  LYS E 641   N  GLU E 616           
SHEET    3 AD1 3 ASP E 647  LEU E 648 -1  O  LEU E 648   N  VAL E 640           
SHEET    1 AD2 3 PRO E 656  GLY E 658  0                                        
SHEET    2 AD2 3 MET E 661  CYS E 663 -1  O  MET E 661   N  GLY E 658           
SHEET    3 AD2 3 CYS E 668  PRO E 670 -1  O  LEU E 669   N  MET E 662           
SHEET    1 AD3 2 GLY E 692  CYS E 694  0                                        
SHEET    2 AD3 2 CYS E 700  CYS E 702 -1  O  VAL E 701   N  VAL E 693           
SHEET    1 AD4 2 TRP E 706  ILE E 707  0                                        
SHEET    2 AD4 2 THR E 713  TYR E 714 -1  O  THR E 713   N  ILE E 707           
SHEET    1 AD5 5 THR G 283  THR G 292  0                                        
SHEET    2 AD5 5 LYS G 239  ASN G 247  1  N  LEU G 243   O  VAL G 286           
SHEET    3 AD5 5 ALA G 326  SER G 331  1  O  PHE G 330   N  VAL G 246           
SHEET    4 AD5 5 GLY G 355  GLU G 359  1  O  ASN G 358   N  SER G 331           
SHEET    5 AD5 5 GLY G 341  ALA G 343 -1  N  ALA G 342   O  VAL G 357           
SHEET    1 AD6 2 CYS G 491  LYS G 492  0                                        
SHEET    2 AD6 2 LYS G 495  PHE G 496 -1  O  LYS G 495   N  LYS G 492           
SHEET    1 AD7 2 VAL G 502  ARG G 504  0                                        
SHEET    2 AD7 2 GLU G 514  THR G 515 -1  O  GLU G 514   N  ARG G 504           
SHEET    1 AD8 3 SER G 534  CYS G 535  0                                        
SHEET    2 AD8 3 GLY G 540  PHE G 543 -1  O  GLY G 540   N  CYS G 535           
SHEET    3 AD8 3 ARG G 546  LYS G 548 -1  O  ARG G 546   N  PHE G 543           
SHEET    1 AD9 2 THR G 563  ALA G 564  0                                        
SHEET    2 AD9 2 CYS G 605  THR G 606 -1  O  THR G 606   N  THR G 563           
SHEET    1 AE1 3 GLU G 616  LEU G 617  0                                        
SHEET    2 AE1 3 VAL G 640  LYS G 641 -1  O  LYS G 641   N  GLU G 616           
SHEET    3 AE1 3 ASP G 647  LEU G 648 -1  O  LEU G 648   N  VAL G 640           
SHEET    1 AE2 3 PRO G 656  GLY G 658  0                                        
SHEET    2 AE2 3 MET G 661  CYS G 663 -1  O  MET G 661   N  CYS G 657           
SHEET    3 AE2 3 CYS G 668  PRO G 670 -1  O  LEU G 669   N  MET G 662           
SHEET    1 AE3 2 GLY G 692  CYS G 694  0                                        
SHEET    2 AE3 2 CYS G 700  CYS G 702 -1  O  VAL G 701   N  VAL G 693           
SHEET    1 AE4 2 TRP G 706  ILE G 707  0                                        
SHEET    2 AE4 2 THR G 713  TYR G 714 -1  O  THR G 713   N  ILE G 707           
SHEET    1 AE5 5 THR I 283  THR I 292  0                                        
SHEET    2 AE5 5 LYS I 239  ASN I 247  1  N  ILE I 241   O  ARG I 284           
SHEET    3 AE5 5 ALA I 326  SER I 331  1  O  PHE I 330   N  VAL I 246           
SHEET    4 AE5 5 GLY I 355  GLU I 359  1  O  ASN I 358   N  SER I 331           
SHEET    5 AE5 5 GLY I 341  ALA I 343 -1  N  ALA I 342   O  VAL I 357           
SHEET    1 AE6 2 CYS I 491  LYS I 492  0                                        
SHEET    2 AE6 2 LYS I 495  PHE I 496 -1  O  LYS I 495   N  LYS I 492           
SHEET    1 AE7 2 VAL I 502  ARG I 504  0                                        
SHEET    2 AE7 2 GLU I 514  THR I 515 -1  O  GLU I 514   N  ARG I 504           
SHEET    1 AE8 3 SER I 534  CYS I 535  0                                        
SHEET    2 AE8 3 GLY I 540  PHE I 543 -1  O  GLY I 540   N  CYS I 535           
SHEET    3 AE8 3 ARG I 546  LYS I 548 -1  O  ARG I 546   N  PHE I 543           
SHEET    1 AE9 2 THR I 563  ALA I 564  0                                        
SHEET    2 AE9 2 CYS I 605  THR I 606 -1  O  THR I 606   N  THR I 563           
SHEET    1 AF1 3 GLU I 616  LEU I 617  0                                        
SHEET    2 AF1 3 VAL I 640  LYS I 641 -1  O  LYS I 641   N  GLU I 616           
SHEET    3 AF1 3 ASP I 647  LEU I 648 -1  O  LEU I 648   N  VAL I 640           
SHEET    1 AF2 2 THR I 622  LEU I 625  0                                        
SHEET    2 AF2 2 ASN I 634  GLY I 637 -1  O  CYS I 635   N  THR I 624           
SHEET    1 AF3 3 PRO I 656  GLY I 658  0                                        
SHEET    2 AF3 3 MET I 661  CYS I 663 -1  O  MET I 661   N  GLY I 658           
SHEET    3 AF3 3 CYS I 668  PRO I 670 -1  O  LEU I 669   N  MET I 662           
SHEET    1 AF4 2 GLY I 692  CYS I 694  0                                        
SHEET    2 AF4 2 CYS I 700  CYS I 702 -1  O  VAL I 701   N  VAL I 693           
SHEET    1 AF5 2 TRP I 706  ILE I 707  0                                        
SHEET    2 AF5 2 THR I 713  TYR I 714 -1  O  THR I 713   N  ILE I 707           
SHEET    1 AF6 5 THR K 283  THR K 292  0                                        
SHEET    2 AF6 5 LYS K 239  ASN K 247  1  N  ILE K 241   O  ARG K 284           
SHEET    3 AF6 5 ALA K 326  SER K 331  1  O  PHE K 330   N  VAL K 246           
SHEET    4 AF6 5 GLY K 355  GLU K 359  1  O  ASN K 358   N  SER K 331           
SHEET    5 AF6 5 GLY K 341  ALA K 343 -1  N  ALA K 342   O  VAL K 357           
SHEET    1 AF7 2 CYS K 474  LYS K 475  0                                        
SHEET    2 AF7 2 THR K 478  LEU K 479 -1  O  THR K 478   N  LYS K 475           
SHEET    1 AF8 2 CYS K 491  LYS K 492  0                                        
SHEET    2 AF8 2 LYS K 495  PHE K 496 -1  O  LYS K 495   N  LYS K 492           
SHEET    1 AF9 2 VAL K 502  ARG K 504  0                                        
SHEET    2 AF9 2 GLU K 514  THR K 515 -1  O  GLU K 514   N  ARG K 504           
SHEET    1 AG1 3 SER K 534  CYS K 535  0                                        
SHEET    2 AG1 3 GLY K 540  PHE K 543 -1  O  GLY K 540   N  CYS K 535           
SHEET    3 AG1 3 ARG K 546  LYS K 548 -1  O  ARG K 546   N  PHE K 543           
SHEET    1 AG2 2 THR K 563  ALA K 564  0                                        
SHEET    2 AG2 2 CYS K 605  THR K 606 -1  O  THR K 606   N  THR K 563           
SHEET    1 AG3 2 LYS K 585  ASP K 586  0                                        
SHEET    2 AG3 2 THR K 589  TRP K 590 -1  O  THR K 589   N  ASP K 586           
SHEET    1 AG4 3 GLU K 616  LEU K 617  0                                        
SHEET    2 AG4 3 VAL K 640  LYS K 641 -1  O  LYS K 641   N  GLU K 616           
SHEET    3 AG4 3 ASP K 647  LEU K 648 -1  O  LEU K 648   N  VAL K 640           
SHEET    1 AG5 2 SER K 623  GLN K 628  0                                        
SHEET    2 AG5 2 ARG K 631  SER K 636 -1  O  CYS K 635   N  THR K 624           
SHEET    1 AG6 3 PRO K 656  GLY K 658  0                                        
SHEET    2 AG6 3 MET K 661  CYS K 663 -1  O  MET K 661   N  GLY K 658           
SHEET    3 AG6 3 CYS K 668  PRO K 670 -1  O  LEU K 669   N  MET K 662           
SHEET    1 AG7 2 GLY K 692  CYS K 694  0                                        
SHEET    2 AG7 2 CYS K 700  CYS K 702 -1  O  VAL K 701   N  VAL K 693           
SHEET    1 AG8 2 TRP K 706  ILE K 707  0                                        
SHEET    2 AG8 2 THR K 713  TYR K 714 -1  O  THR K 713   N  ILE K 707           
SHEET    1 AG9 4 GLU B 225  LEU B 232  0                                        
SHEET    2 AG9 4 THR B 545  VAL B 551 -1  O  LYS B 549   N  ALA B 227           
SHEET    3 AG9 4 ARG B 533  SER B 540 -1  N  ALA B 538   O  GLN B 546           
SHEET    4 AG9 4 PRO B 522  ILE B 530 -1  N  VAL B 528   O  PHE B 535           
SHEET    1 AH1 4 ILE B 239  TYR B 244  0                                        
SHEET    2 AH1 4 ASP B 247  ALA B 253 -1  O  VAL B 251   N  ASP B 240           
SHEET    3 AH1 4 LYS B 259  ASP B 266 -1  O  LEU B 263   N  VAL B 250           
SHEET    4 AH1 4 THR B 271  THR B 279 -1  O  ARG B 273   N  GLU B 264           
SHEET    1 AH2 4 THR B 283  ILE B 291  0                                        
SHEET    2 AH2 4 GLN B 294  GLN B 301 -1  O  TYR B 296   N  ILE B 289           
SHEET    3 AH2 4 HIS B 307  ASP B 312 -1  O  TYR B 309   N  VAL B 297           
SHEET    4 AH2 4 LYS B 317  ASP B 323 -1  O  LYS B 317   N  ASP B 312           
SHEET    1 AH3 4 PRO B 332  ILE B 340  0                                        
SHEET    2 AH3 4 ASN B 343  ASP B 350 -1  O  ALA B 349   N  ASP B 334           
SHEET    3 AH3 4 THR B 357  TRP B 362 -1  O  TYR B 360   N  PHE B 346           
SHEET    4 AH3 4 PHE B 367  LEU B 373 -1  O  GLN B 371   N  ILE B 359           
SHEET    1 AH4 4 ASP B 379  ILE B 387  0                                        
SHEET    2 AH4 4 THR B 396  SER B 403 -1  O  SER B 402   N  THR B 380           
SHEET    3 AH4 4 VAL B 409  ASN B 414 -1  O  TYR B 411   N  LEU B 399           
SHEET    4 AH4 4 LEU B 419  ASP B 425 -1  O  THR B 424   N  ILE B 410           
SHEET    1 AH5 4 ALA B 434  VAL B 440  0                                        
SHEET    2 AH5 4 ASP B 443  THR B 449 -1  O  CYS B 447   N  LYS B 436           
SHEET    3 AH5 4 ILE B 452  GLY B 461 -1  O  TRP B 460   N  VAL B 444           
SHEET    4 AH5 4 SER B 464  ARG B 474 -1  O  SER B 473   N  GLY B 453           
SHEET    1 AH6 4 PHE B 479  ILE B 484  0                                        
SHEET    2 AH6 4 TYR B 487  LEU B 492 -1  O  TYR B 489   N  LEU B 482           
SHEET    3 AH6 4 THR B 499  ASP B 505 -1  O  TYR B 502   N  ALA B 490           
SHEET    4 AH6 4 LYS B 510  LEU B 517 -1  O  VAL B 512   N  ASN B 503           
SHEET    1 AH7 4 GLU D 225  LEU D 232  0                                        
SHEET    2 AH7 4 THR D 545  VAL D 551 -1  O  LYS D 549   N  ALA D 227           
SHEET    3 AH7 4 ARG D 533  SER D 540 -1  N  ALA D 538   O  GLN D 546           
SHEET    4 AH7 4 PRO D 522  ILE D 530 -1  N  ILE D 530   O  ARG D 533           
SHEET    1 AH8 4 ILE D 239  TYR D 244  0                                        
SHEET    2 AH8 4 ASP D 247  ALA D 253 -1  O  VAL D 251   N  ASP D 240           
SHEET    3 AH8 4 LYS D 259  ASP D 266 -1  O  LEU D 263   N  VAL D 250           
SHEET    4 AH8 4 THR D 271  THR D 279 -1  O  ARG D 273   N  GLU D 264           
SHEET    1 AH9 4 THR D 283  ILE D 291  0                                        
SHEET    2 AH9 4 GLN D 294  GLN D 301 -1  O  TYR D 296   N  ILE D 289           
SHEET    3 AH9 4 HIS D 307  ASP D 312 -1  O  TYR D 309   N  VAL D 297           
SHEET    4 AH9 4 LYS D 317  ASP D 323 -1  O  LYS D 317   N  ASP D 312           
SHEET    1 AI1 4 PRO D 332  ILE D 340  0                                        
SHEET    2 AI1 4 ASN D 343  ASP D 350 -1  O  ALA D 349   N  ASP D 334           
SHEET    3 AI1 4 THR D 357  TRP D 362 -1  O  TRP D 362   N  TRP D 344           
SHEET    4 AI1 4 PHE D 367  LEU D 373 -1  O  GLN D 371   N  ILE D 359           
SHEET    1 AI2 4 ASP D 379  ILE D 387  0                                        
SHEET    2 AI2 4 THR D 396  SER D 403 -1  O  SER D 402   N  THR D 380           
SHEET    3 AI2 4 VAL D 409  ASN D 414 -1  O  TYR D 411   N  LEU D 399           
SHEET    4 AI2 4 LEU D 419  ASP D 425 -1  O  THR D 421   N  GLN D 412           
SHEET    1 AI3 4 ALA D 434  VAL D 440  0                                        
SHEET    2 AI3 4 ASP D 443  THR D 449 -1  O  TYR D 445   N  PHE D 438           
SHEET    3 AI3 4 ILE D 452  TRP D 460 -1  O  TRP D 460   N  VAL D 444           
SHEET    4 AI3 4 PHE D 465  ARG D 474 -1  O  MET D 471   N  SER D 455           
SHEET    1 AI4 4 PHE D 479  ILE D 484  0                                        
SHEET    2 AI4 4 TYR D 487  LEU D 492 -1  O  TYR D 489   N  LEU D 482           
SHEET    3 AI4 4 THR D 499  ASP D 505 -1  O  TYR D 502   N  ALA D 490           
SHEET    4 AI4 4 LYS D 510  LEU D 517 -1  O  LYS D 510   N  ASP D 505           
SHEET    1 AI5 4 GLU F 225  LEU F 232  0                                        
SHEET    2 AI5 4 THR F 545  VAL F 551 -1  O  LYS F 549   N  ALA F 227           
SHEET    3 AI5 4 ARG F 533  SER F 540 -1  N  ALA F 538   O  GLN F 546           
SHEET    4 AI5 4 PRO F 522  ILE F 530 -1  N  ILE F 530   O  ARG F 533           
SHEET    1 AI6 4 ILE F 239  TYR F 244  0                                        
SHEET    2 AI6 4 ASP F 247  ALA F 253 -1  O  VAL F 251   N  ASP F 240           
SHEET    3 AI6 4 CYS F 260  TRP F 265 -1  O  LEU F 263   N  VAL F 250           
SHEET    4 AI6 4 PHE F 272  ASP F 276 -1  O  ARG F 273   N  GLU F 264           
SHEET    1 AI7 4 THR F 283  ILE F 291  0                                        
SHEET    2 AI7 4 GLN F 294  GLN F 301 -1  O  ALA F 300   N  VAL F 284           
SHEET    3 AI7 4 HIS F 307  ASP F 312 -1  O  TYR F 309   N  VAL F 297           
SHEET    4 AI7 4 LYS F 317  ASP F 323 -1  O  ILE F 319   N  LYS F 310           
SHEET    1 AI8 4 PRO F 332  ILE F 340  0                                        
SHEET    2 AI8 4 ASN F 343  ASP F 350 -1  O  ALA F 349   N  ASP F 334           
SHEET    3 AI8 4 THR F 357  TRP F 362 -1  O  TYR F 360   N  PHE F 346           
SHEET    4 AI8 4 PHE F 367  LEU F 373 -1  O  GLN F 371   N  ILE F 359           
SHEET    1 AI9 4 ASP F 379  ILE F 387  0                                        
SHEET    2 AI9 4 THR F 396  SER F 403 -1  O  SER F 402   N  THR F 380           
SHEET    3 AI9 4 VAL F 409  ASN F 414 -1  O  TYR F 411   N  LEU F 399           
SHEET    4 AI9 4 LEU F 419  ASP F 425 -1  O  THR F 424   N  ILE F 410           
SHEET    1 AJ1 4 ALA F 434  VAL F 440  0                                        
SHEET    2 AJ1 4 ASP F 443  THR F 449 -1  O  TYR F 445   N  PHE F 438           
SHEET    3 AJ1 4 ILE F 452  TRP F 460 -1  O  LYS F 456   N  LEU F 448           
SHEET    4 AJ1 4 PHE F 465  ARG F 474 -1  O  SER F 473   N  GLY F 453           
SHEET    1 AJ2 4 PHE F 479  ILE F 484  0                                        
SHEET    2 AJ2 4 TYR F 487  LEU F 492 -1  O  TYR F 489   N  LEU F 482           
SHEET    3 AJ2 4 THR F 499  ASP F 505 -1  O  TYR F 502   N  ALA F 490           
SHEET    4 AJ2 4 LYS F 510  LEU F 517 -1  O  LYS F 510   N  ASP F 505           
SHEET    1 AJ3 4 GLU H 225  LEU H 232  0                                        
SHEET    2 AJ3 4 THR H 545  VAL H 551 -1  O  LYS H 549   N  ALA H 227           
SHEET    3 AJ3 4 ARG H 533  SER H 540 -1  N  ALA H 538   O  GLN H 546           
SHEET    4 AJ3 4 PRO H 522  ILE H 530 -1  N  VAL H 528   O  PHE H 535           
SHEET    1 AJ4 4 ILE H 239  TYR H 244  0                                        
SHEET    2 AJ4 4 ASP H 247  ALA H 253 -1  O  VAL H 251   N  ASP H 240           
SHEET    3 AJ4 4 LYS H 259  ASP H 266 -1  O  LEU H 263   N  VAL H 250           
SHEET    4 AJ4 4 THR H 271  THR H 279 -1  O  ASP H 276   N  PHE H 262           
SHEET    1 AJ5 4 THR H 283  ILE H 291  0                                        
SHEET    2 AJ5 4 GLN H 294  GLN H 301 -1  O  TYR H 296   N  ILE H 289           
SHEET    3 AJ5 4 HIS H 307  ASP H 312 -1  O  TYR H 309   N  VAL H 297           
SHEET    4 AJ5 4 LYS H 317  ASP H 323 -1  O  GLN H 322   N  ILE H 308           
SHEET    1 AJ6 4 PRO H 332  ILE H 340  0                                        
SHEET    2 AJ6 4 ASN H 343  ASP H 350 -1  O  ALA H 349   N  ASP H 334           
SHEET    3 AJ6 4 THR H 357  TRP H 362 -1  O  TRP H 362   N  TRP H 344           
SHEET    4 AJ6 4 PHE H 367  LEU H 373 -1  O  GLN H 371   N  ILE H 359           
SHEET    1 AJ7 4 ASP H 379  ILE H 387  0                                        
SHEET    2 AJ7 4 THR H 396  SER H 403 -1  O  SER H 402   N  THR H 380           
SHEET    3 AJ7 4 VAL H 409  ASN H 414 -1  O  TYR H 411   N  LEU H 399           
SHEET    4 AJ7 4 LEU H 419  ASP H 425 -1  O  THR H 421   N  GLN H 412           
SHEET    1 AJ8 4 ALA H 434  VAL H 440  0                                        
SHEET    2 AJ8 4 ASP H 443  THR H 449 -1  O  CYS H 447   N  LYS H 436           
SHEET    3 AJ8 4 ILE H 452  TRP H 460 -1  O  LYS H 456   N  LEU H 448           
SHEET    4 AJ8 4 PHE H 465  ARG H 474 -1  O  SER H 473   N  GLY H 453           
SHEET    1 AJ9 4 PHE H 479  ILE H 484  0                                        
SHEET    2 AJ9 4 TYR H 487  LEU H 492 -1  O  TYR H 489   N  LEU H 482           
SHEET    3 AJ9 4 THR H 499  ASP H 505 -1  O  TYR H 502   N  ALA H 490           
SHEET    4 AJ9 4 LYS H 510  LEU H 517 -1  O  GLN H 515   N  VAL H 501           
SHEET    1 AK1 4 GLU J 225  LEU J 232  0                                        
SHEET    2 AK1 4 THR J 545  VAL J 551 -1  O  LYS J 549   N  ALA J 227           
SHEET    3 AK1 4 ARG J 533  SER J 540 -1  N  ALA J 538   O  GLN J 546           
SHEET    4 AK1 4 PRO J 522  ILE J 530 -1  N  VAL J 528   O  PHE J 535           
SHEET    1 AK2 4 ILE J 239  TYR J 244  0                                        
SHEET    2 AK2 4 ASP J 247  ALA J 253 -1  O  VAL J 251   N  ASP J 240           
SHEET    3 AK2 4 LYS J 259  TRP J 265 -1  O  LEU J 263   N  VAL J 250           
SHEET    4 AK2 4 PHE J 272  THR J 279 -1  O  ASP J 276   N  PHE J 262           
SHEET    1 AK3 4 THR J 283  ILE J 291  0                                        
SHEET    2 AK3 4 GLN J 294  GLN J 301 -1  O  TYR J 296   N  ILE J 289           
SHEET    3 AK3 4 HIS J 307  ASP J 312 -1  O  TYR J 309   N  VAL J 297           
SHEET    4 AK3 4 LYS J 317  ASP J 323 -1  O  GLN J 322   N  ILE J 308           
SHEET    1 AK4 4 PRO J 332  ILE J 340  0                                        
SHEET    2 AK4 4 ASN J 343  ASP J 350 -1  O  ALA J 349   N  ASP J 334           
SHEET    3 AK4 4 THR J 357  TRP J 362 -1  O  TRP J 362   N  TRP J 344           
SHEET    4 AK4 4 PHE J 367  LEU J 373 -1  O  GLN J 371   N  ILE J 359           
SHEET    1 AK5 4 ASP J 379  ILE J 387  0                                        
SHEET    2 AK5 4 THR J 396  SER J 403 -1  O  SER J 402   N  THR J 380           
SHEET    3 AK5 4 VAL J 409  ASN J 414 -1  O  TYR J 411   N  LEU J 399           
SHEET    4 AK5 4 LEU J 419  ASP J 425 -1  O  THR J 424   N  ILE J 410           
SHEET    1 AK6 4 ALA J 434  VAL J 440  0                                        
SHEET    2 AK6 4 ASP J 443  THR J 449 -1  O  CYS J 447   N  LYS J 436           
SHEET    3 AK6 4 ILE J 452  TRP J 460 -1  O  TRP J 460   N  VAL J 444           
SHEET    4 AK6 4 PHE J 465  ARG J 474 -1  O  SER J 473   N  GLY J 453           
SHEET    1 AK7 4 PHE J 479  ILE J 484  0                                        
SHEET    2 AK7 4 TYR J 487  LEU J 492 -1  O  TYR J 489   N  LEU J 482           
SHEET    3 AK7 4 THR J 499  ASP J 505 -1  O  TYR J 502   N  ALA J 490           
SHEET    4 AK7 4 LYS J 510  LEU J 517 -1  O  LEU J 517   N  THR J 499           
SHEET    1 AK8 4 GLU L 225  LEU L 232  0                                        
SHEET    2 AK8 4 THR L 545  VAL L 551 -1  O  LYS L 549   N  ALA L 227           
SHEET    3 AK8 4 ARG L 533  SER L 540 -1  N  ALA L 538   O  GLN L 546           
SHEET    4 AK8 4 PRO L 522  ILE L 530 -1  N  VAL L 528   O  PHE L 535           
SHEET    1 AK9 4 ILE L 239  SER L 243  0                                        
SHEET    2 AK9 4 GLU L 248  ALA L 253 -1  O  VAL L 251   N  ASP L 240           
SHEET    3 AK9 4 LYS L 259  ASP L 266 -1  O  LEU L 263   N  VAL L 250           
SHEET    4 AK9 4 THR L 271  THR L 279 -1  O  ARG L 273   N  GLU L 264           
SHEET    1 AL1 4 THR L 283  ILE L 291  0                                        
SHEET    2 AL1 4 GLN L 294  GLN L 301 -1  O  TYR L 296   N  ILE L 289           
SHEET    3 AL1 4 HIS L 307  ASP L 312 -1  O  TYR L 309   N  VAL L 297           
SHEET    4 AL1 4 LYS L 317  ASP L 323 -1  O  GLN L 322   N  ILE L 308           
SHEET    1 AL2 4 PRO L 332  ILE L 340  0                                        
SHEET    2 AL2 4 ASN L 343  ASP L 350 -1  O  ALA L 349   N  ASP L 334           
SHEET    3 AL2 4 THR L 357  TRP L 362 -1  O  TRP L 362   N  TRP L 344           
SHEET    4 AL2 4 PHE L 367  LEU L 373 -1  O  GLN L 371   N  ILE L 359           
SHEET    1 AL3 4 ASP L 379  ILE L 387  0                                        
SHEET    2 AL3 4 THR L 396  SER L 403 -1  O  SER L 402   N  THR L 380           
SHEET    3 AL3 4 VAL L 409  ASN L 414 -1  O  TYR L 411   N  LEU L 399           
SHEET    4 AL3 4 LEU L 419  ASP L 425 -1  O  THR L 424   N  ILE L 410           
SHEET    1 AL4 4 ALA L 434  VAL L 440  0                                        
SHEET    2 AL4 4 ASP L 443  THR L 449 -1  O  CYS L 447   N  LYS L 436           
SHEET    3 AL4 4 ILE L 452  TRP L 460 -1  O  LYS L 456   N  LEU L 448           
SHEET    4 AL4 4 PHE L 465  ARG L 474 -1  O  GLN L 466   N  LYS L 459           
SHEET    1 AL5 4 PHE L 479  ILE L 484  0                                        
SHEET    2 AL5 4 TYR L 487  LEU L 492 -1  O  TYR L 489   N  LEU L 482           
SHEET    3 AL5 4 THR L 499  ASP L 505 -1  O  TYR L 502   N  ALA L 490           
SHEET    4 AL5 4 LYS L 510  LEU L 517 -1  O  LYS L 510   N  ASP L 505           
SSBOND   1 CYS A  349    CYS A  433                          1555   1555  2.03  
SSBOND   2 CYS A  392    CYS A  417                          1555   1555  2.03  
SSBOND   3 CYS A  394    CYS A  401                          1555   1555  2.03  
SSBOND   4 CYS A  447    CYS A  477                          1555   1555  2.03  
SSBOND   5 CYS A  458    CYS A  474                          1555   1555  2.03  
SSBOND   6 CYS A  460    CYS A  466                          1555   1555  2.04  
SSBOND   7 CYS A  473    CYS A  494                          1555   1555  2.03  
SSBOND   8 CYS A  485    CYS A  491                          1555   1555  2.03  
SSBOND   9 CYS A  490    CYS A  516                          1555   1555  2.03  
SSBOND  10 CYS A  503    CYS A  523                          1555   1555  2.03  
SSBOND  11 CYS A  510    CYS A  542                          1555   1555  2.03  
SSBOND  12 CYS A  535    CYS A  547                          1555   1555  2.03  
SSBOND  13 CYS A  554    CYS A  605                          1555   1555  2.03  
SSBOND  14 CYS A  569    CYS A  635                          1555   1555  2.03  
SSBOND  15 CYS A  583    CYS A  593                          1555   1555  2.03  
SSBOND  16 CYS A  600    CYS A  663                          1555   1555  2.03  
SSBOND  17 CYS A  657    CYS A  668                          1555   1555  2.03  
SSBOND  18 CYS A  679    CYS A  694                          1555   1555  2.03  
SSBOND  19 CYS A  688    CYS A  700                          1555   1555  2.03  
SSBOND  20 CYS A  702    CYS A  711                          1555   1555  2.03  
SSBOND  21 CYS C  349    CYS C  433                          1555   1555  2.03  
SSBOND  22 CYS C  392    CYS C  417                          1555   1555  2.03  
SSBOND  23 CYS C  394    CYS C  401                          1555   1555  2.03  
SSBOND  24 CYS C  447    CYS C  477                          1555   1555  2.03  
SSBOND  25 CYS C  458    CYS C  474                          1555   1555  2.03  
SSBOND  26 CYS C  460    CYS C  466                          1555   1555  2.03  
SSBOND  27 CYS C  473    CYS C  494                          1555   1555  2.03  
SSBOND  28 CYS C  485    CYS C  491                          1555   1555  2.03  
SSBOND  29 CYS C  490    CYS C  516                          1555   1555  2.03  
SSBOND  30 CYS C  503    CYS C  523                          1555   1555  2.03  
SSBOND  31 CYS C  510    CYS C  542                          1555   1555  2.03  
SSBOND  32 CYS C  535    CYS C  547                          1555   1555  2.03  
SSBOND  33 CYS C  554    CYS C  605                          1555   1555  2.03  
SSBOND  34 CYS C  569    CYS C  635                          1555   1555  2.03  
SSBOND  35 CYS C  583    CYS C  593                          1555   1555  2.03  
SSBOND  36 CYS C  600    CYS C  663                          1555   1555  2.03  
SSBOND  37 CYS C  657    CYS C  668                          1555   1555  2.03  
SSBOND  38 CYS C  679    CYS C  694                          1555   1555  2.03  
SSBOND  39 CYS C  688    CYS C  700                          1555   1555  2.03  
SSBOND  40 CYS C  702    CYS C  711                          1555   1555  2.03  
SSBOND  41 CYS E  349    CYS E  433                          1555   1555  2.03  
SSBOND  42 CYS E  392    CYS E  417                          1555   1555  2.03  
SSBOND  43 CYS E  394    CYS E  401                          1555   1555  2.03  
SSBOND  44 CYS E  447    CYS E  477                          1555   1555  2.03  
SSBOND  45 CYS E  458    CYS E  474                          1555   1555  2.02  
SSBOND  46 CYS E  460    CYS E  466                          1555   1555  2.02  
SSBOND  47 CYS E  473    CYS E  494                          1555   1555  2.03  
SSBOND  48 CYS E  485    CYS E  491                          1555   1555  2.03  
SSBOND  49 CYS E  490    CYS E  516                          1555   1555  2.03  
SSBOND  50 CYS E  503    CYS E  523                          1555   1555  2.03  
SSBOND  51 CYS E  510    CYS E  542                          1555   1555  2.03  
SSBOND  52 CYS E  535    CYS E  547                          1555   1555  2.03  
SSBOND  53 CYS E  554    CYS E  605                          1555   1555  2.03  
SSBOND  54 CYS E  569    CYS E  635                          1555   1555  2.03  
SSBOND  55 CYS E  583    CYS E  593                          1555   1555  2.05  
SSBOND  56 CYS E  600    CYS E  663                          1555   1555  2.03  
SSBOND  57 CYS E  657    CYS E  668                          1555   1555  2.03  
SSBOND  58 CYS E  679    CYS E  694                          1555   1555  2.03  
SSBOND  59 CYS E  688    CYS E  700                          1555   1555  2.04  
SSBOND  60 CYS E  702    CYS E  711                          1555   1555  2.03  
SSBOND  61 CYS G  349    CYS G  433                          1555   1555  2.03  
SSBOND  62 CYS G  392    CYS G  417                          1555   1555  2.03  
SSBOND  63 CYS G  394    CYS G  401                          1555   1555  2.03  
SSBOND  64 CYS G  447    CYS G  477                          1555   1555  2.03  
SSBOND  65 CYS G  458    CYS G  474                          1555   1555  2.03  
SSBOND  66 CYS G  460    CYS G  466                          1555   1555  2.03  
SSBOND  67 CYS G  473    CYS G  494                          1555   1555  2.03  
SSBOND  68 CYS G  485    CYS G  491                          1555   1555  2.03  
SSBOND  69 CYS G  490    CYS G  516                          1555   1555  2.03  
SSBOND  70 CYS G  503    CYS G  523                          1555   1555  2.04  
SSBOND  71 CYS G  510    CYS G  542                          1555   1555  2.03  
SSBOND  72 CYS G  535    CYS G  547                          1555   1555  2.03  
SSBOND  73 CYS G  554    CYS G  605                          1555   1555  2.03  
SSBOND  74 CYS G  569    CYS G  635                          1555   1555  2.03  
SSBOND  75 CYS G  583    CYS G  593                          1555   1555  2.02  
SSBOND  76 CYS G  600    CYS G  663                          1555   1555  2.03  
SSBOND  77 CYS G  657    CYS G  668                          1555   1555  2.03  
SSBOND  78 CYS G  679    CYS G  694                          1555   1555  2.03  
SSBOND  79 CYS G  688    CYS G  700                          1555   1555  2.03  
SSBOND  80 CYS G  702    CYS G  711                          1555   1555  2.03  
SSBOND  81 CYS I  349    CYS I  433                          1555   1555  2.04  
SSBOND  82 CYS I  392    CYS I  417                          1555   1555  2.03  
SSBOND  83 CYS I  394    CYS I  401                          1555   1555  2.03  
SSBOND  84 CYS I  447    CYS I  477                          1555   1555  2.03  
SSBOND  85 CYS I  458    CYS I  474                          1555   1555  2.03  
SSBOND  86 CYS I  460    CYS I  466                          1555   1555  2.04  
SSBOND  87 CYS I  473    CYS I  494                          1555   1555  2.03  
SSBOND  88 CYS I  485    CYS I  491                          1555   1555  2.03  
SSBOND  89 CYS I  490    CYS I  516                          1555   1555  2.03  
SSBOND  90 CYS I  503    CYS I  523                          1555   1555  2.03  
SSBOND  91 CYS I  510    CYS I  542                          1555   1555  2.03  
SSBOND  92 CYS I  535    CYS I  547                          1555   1555  2.03  
SSBOND  93 CYS I  554    CYS I  605                          1555   1555  2.03  
SSBOND  94 CYS I  569    CYS I  635                          1555   1555  2.03  
SSBOND  95 CYS I  583    CYS I  593                          1555   1555  2.03  
SSBOND  96 CYS I  600    CYS I  663                          1555   1555  2.03  
SSBOND  97 CYS I  657    CYS I  668                          1555   1555  2.03  
SSBOND  98 CYS I  679    CYS I  694                          1555   1555  2.03  
SSBOND  99 CYS I  688    CYS I  700                          1555   1555  2.03  
SSBOND 100 CYS I  702    CYS I  711                          1555   1555  2.03  
SSBOND 101 CYS K  349    CYS K  433                          1555   1555  2.03  
SSBOND 102 CYS K  392    CYS K  417                          1555   1555  2.03  
SSBOND 103 CYS K  394    CYS K  401                          1555   1555  2.03  
SSBOND 104 CYS K  447    CYS K  477                          1555   1555  2.03  
SSBOND 105 CYS K  458    CYS K  474                          1555   1555  2.03  
SSBOND 106 CYS K  460    CYS K  466                          1555   1555  2.03  
SSBOND 107 CYS K  473    CYS K  494                          1555   1555  2.03  
SSBOND 108 CYS K  485    CYS K  491                          1555   1555  2.03  
SSBOND 109 CYS K  490    CYS K  516                          1555   1555  2.03  
SSBOND 110 CYS K  503    CYS K  523                          1555   1555  2.03  
SSBOND 111 CYS K  510    CYS K  542                          1555   1555  2.04  
SSBOND 112 CYS K  535    CYS K  547                          1555   1555  2.03  
SSBOND 113 CYS K  554    CYS K  605                          1555   1555  2.03  
SSBOND 114 CYS K  569    CYS K  635                          1555   1555  2.03  
SSBOND 115 CYS K  583    CYS K  593                          1555   1555  2.03  
SSBOND 116 CYS K  600    CYS K  663                          1555   1555  2.03  
SSBOND 117 CYS K  657    CYS K  668                          1555   1555  2.03  
SSBOND 118 CYS K  679    CYS K  694                          1555   1555  2.03  
SSBOND 119 CYS K  688    CYS K  700                          1555   1555  2.03  
SSBOND 120 CYS K  702    CYS K  711                          1555   1555  2.03  
SSBOND 121 CYS B  260    CYS B  286                          1555   1555  2.03  
SSBOND 122 CYS D  260    CYS D  286                          1555   1555  2.03  
SSBOND 123 CYS F  260    CYS F  286                          1555   1555  2.03  
SSBOND 124 CYS H  260    CYS H  286                          1555   1555  2.02  
SSBOND 125 CYS J  260    CYS J  286                          1555   1555  2.03  
SSBOND 126 CYS L  260    CYS L  286                          1555   1555  2.03  
LINK         OE2 GLU A 242                CA    CA A 801     1555   1555  2.37  
LINK         OD1 ASP A 325                CA    CA A 801     1555   1555  2.37  
LINK         OD2 ASP A 325                CA    CA A 801     1555   1555  2.36  
LINK         O   CYS A 433                CA    CA A 801     1555   1555  2.38  
LINK         OD1 ASN A 436                CA    CA A 801     1555   1555  2.38  
LINK         O   GLU A 446                CA    CA A 802     1555   1555  2.36  
LINK         OD1 ASN A 449                CA    CA A 802     1555   1555  2.37  
LINK         O   PHE A 451                CA    CA A 802     1555   1555  2.39  
LINK         OE1 GLU A 453                CA    CA A 802     1555   1555  2.36  
LINK         OE1 GLU A 456                CA    CA A 802     1555   1555  2.36  
LINK         OD2 ASP A 459                CA    CA A 802     1555   1555  2.37  
LINK         OD1 ASP A 511                CA    CA A 803     1555   1555  2.36  
LINK         OD2 ASP A 511                CA    CA A 803     1555   1555  2.38  
LINK         O   ILE A 512                CA    CA A 803     1555   1555  2.39  
LINK         OE2 GLU A 514                CA    CA A 803     1555   1555  2.37  
LINK         OD1 ASN A 526                CA    CA A 803     1555   1555  2.39  
LINK         O   ILE A 527                CA    CA A 803     1555   1555  2.39  
LINK         OE2 GLU C 242                CA    CA C 801     1555   1555  2.36  
LINK         OD1 ASP C 325                CA    CA C 801     1555   1555  2.37  
LINK         OD2 ASP C 325                CA    CA C 801     1555   1555  2.37  
LINK         O   CYS C 433                CA    CA C 801     1555   1555  2.38  
LINK         OD1 ASN C 436                CA    CA C 801     1555   1555  2.39  
LINK         O   GLU C 446                CA    CA C 802     1555   1555  2.35  
LINK         OD1 ASN C 449                CA    CA C 802     1555   1555  2.38  
LINK         O   PHE C 451                CA    CA C 802     1555   1555  2.40  
LINK         OE1 GLU C 453                CA    CA C 802     1555   1555  2.36  
LINK         OE1 GLU C 456                CA    CA C 802     1555   1555  2.37  
LINK         OE2 GLU C 456                CA    CA C 802     1555   1555  2.38  
LINK         OD2 ASP C 459                CA    CA C 802     1555   1555  2.36  
LINK         OD1 ASP C 511                CA    CA C 803     1555   1555  2.39  
LINK         OD2 ASP C 511                CA    CA C 803     1555   1555  2.39  
LINK         O   ILE C 512                CA    CA C 803     1555   1555  2.38  
LINK         OE2 GLU C 514                CA    CA C 803     1555   1555  2.34  
LINK         OD1 ASN C 526                CA    CA C 803     1555   1555  2.39  
LINK         O   ILE C 527                CA    CA C 803     1555   1555  2.42  
LINK         OE2 GLU E 242                CA    CA E 801     1555   1555  2.35  
LINK         OD1 ASP E 325                CA    CA E 801     1555   1555  2.37  
LINK         OD2 ASP E 325                CA    CA E 801     1555   1555  2.37  
LINK         O   CYS E 433                CA    CA E 801     1555   1555  2.41  
LINK         OD1 ASN E 436                CA    CA E 801     1555   1555  2.40  
LINK         O   GLU E 446                CA    CA E 802     1555   1555  2.34  
LINK         OD1 ASN E 449                CA    CA E 802     1555   1555  2.40  
LINK         O   PHE E 451                CA    CA E 802     1555   1555  2.43  
LINK         OE1 GLU E 453                CA    CA E 802     1555   1555  2.37  
LINK         OE1 GLU E 456                CA    CA E 802     1555   1555  2.33  
LINK         OE2 GLU E 456                CA    CA E 802     1555   1555  2.31  
LINK         OD2 ASP E 459                CA    CA E 802     1555   1555  2.35  
LINK         OD1 ASP E 511                CA    CA E 803     1555   1555  2.35  
LINK         OD2 ASP E 511                CA    CA E 803     1555   1555  2.38  
LINK         O   ILE E 512                CA    CA E 803     1555   1555  2.39  
LINK         OE2 GLU E 514                CA    CA E 803     1555   1555  2.37  
LINK         OD1 ASN E 526                CA    CA E 803     1555   1555  2.38  
LINK         O   ILE E 527                CA    CA E 803     1555   1555  2.38  
LINK         OE2 GLU G 242                CA    CA G 801     1555   1555  2.36  
LINK         OD1 ASP G 325                CA    CA G 801     1555   1555  2.38  
LINK         OD2 ASP G 325                CA    CA G 801     1555   1555  2.36  
LINK         O   CYS G 433                CA    CA G 801     1555   1555  2.41  
LINK         OD1 ASN G 436                CA    CA G 801     1555   1555  2.39  
LINK         O   GLU G 446                CA    CA G 802     1555   1555  2.37  
LINK         OD1 ASN G 449                CA    CA G 802     1555   1555  2.39  
LINK         O   PHE G 451                CA    CA G 802     1555   1555  2.40  
LINK         OE1 GLU G 453                CA    CA G 802     1555   1555  2.36  
LINK         OE1 GLU G 456                CA    CA G 802     1555   1555  2.35  
LINK         OE2 GLU G 456                CA    CA G 802     1555   1555  2.39  
LINK         OD2 ASP G 459                CA    CA G 802     1555   1555  2.36  
LINK         OD1 ASP G 511                CA    CA G 803     1555   1555  2.37  
LINK         OD2 ASP G 511                CA    CA G 803     1555   1555  2.36  
LINK         O   ILE G 512                CA    CA G 803     1555   1555  2.38  
LINK         OE2 GLU G 514                CA    CA G 803     1555   1555  2.35  
LINK         OD1 ASN G 526                CA    CA G 803     1555   1555  2.38  
LINK         O   ILE G 527                CA    CA G 803     1555   1555  2.38  
LINK         OE2 GLU I 242                CA    CA I 801     1555   1555  2.36  
LINK         OD1 ASP I 325                CA    CA I 801     1555   1555  2.38  
LINK         OD2 ASP I 325                CA    CA I 801     1555   1555  2.36  
LINK         O   CYS I 433                CA    CA I 801     1555   1555  2.41  
LINK         OD1 ASN I 436                CA    CA I 801     1555   1555  2.40  
LINK         O   GLU I 446                CA    CA I 802     1555   1555  2.37  
LINK         OD1 ASN I 449                CA    CA I 802     1555   1555  2.38  
LINK         O   PHE I 451                CA    CA I 802     1555   1555  2.40  
LINK         OE1 GLU I 453                CA    CA I 802     1555   1555  2.37  
LINK         OE1 GLU I 456                CA    CA I 802     1555   1555  2.35  
LINK         OE2 GLU I 456                CA    CA I 802     1555   1555  2.38  
LINK         OD2 ASP I 459                CA    CA I 802     1555   1555  2.36  
LINK         OD1 ASP I 511                CA    CA I 803     1555   1555  2.35  
LINK         OD2 ASP I 511                CA    CA I 803     1555   1555  2.38  
LINK         O   ILE I 512                CA    CA I 803     1555   1555  2.38  
LINK         OE2 GLU I 514                CA    CA I 803     1555   1555  2.36  
LINK         OD1 ASN I 526                CA    CA I 803     1555   1555  2.38  
LINK         O   ILE I 527                CA    CA I 803     1555   1555  2.40  
LINK         OE2 GLU K 242                CA    CA K 801     1555   1555  2.37  
LINK         OD1 ASP K 325                CA    CA K 801     1555   1555  2.37  
LINK         OD2 ASP K 325                CA    CA K 801     1555   1555  2.37  
LINK         O   CYS K 433                CA    CA K 801     1555   1555  2.38  
LINK         OD1 ASN K 436                CA    CA K 801     1555   1555  2.38  
LINK         O   GLU K 446                CA    CA K 802     1555   1555  2.37  
LINK         OD1 ASN K 449                CA    CA K 802     1555   1555  2.39  
LINK         O   PHE K 451                CA    CA K 802     1555   1555  2.40  
LINK         OE1 GLU K 453                CA    CA K 802     1555   1555  2.36  
LINK         OE1 GLU K 456                CA    CA K 802     1555   1555  2.35  
LINK         OE2 GLU K 456                CA    CA K 802     1555   1555  2.39  
LINK         OD2 ASP K 459                CA    CA K 802     1555   1555  2.36  
LINK         OD1 ASP K 511                CA    CA K 803     1555   1555  2.35  
LINK         OD2 ASP K 511                CA    CA K 803     1555   1555  2.38  
LINK         O   ILE K 512                CA    CA K 803     1555   1555  2.39  
LINK         OE2 GLU K 514                CA    CA K 803     1555   1555  2.36  
LINK         OD1 ASN K 526                CA    CA K 803     1555   1555  2.39  
LINK         O   ILE K 527                CA    CA K 803     1555   1555  2.39  
LINK         ND2 ASN B 277                 C1  NAG B 602     1555   1555  1.44  
LINK         OD1 ASP B 334                CA    CA B 601     1555   1555  2.50  
LINK         OD2 ASP B 334                CA    CA B 601     1555   1555  2.35  
LINK         OE1 GLU B 336                CA    CA B 601     1555   1555  2.36  
LINK         OD1 ASP B 381                CA    CA B 601     1555   1555  2.36  
LINK         OD2 ASP B 381                CA    CA B 601     1555   1555  2.37  
LINK         O   VAL B 382                CA    CA B 601     1555   1555  2.39  
LINK         ND2 ASN B 422                 C1  NAG B 605     1555   1555  1.44  
LINK         ND2 ASN D 277                 C1  NAG D 602     1555   1555  1.43  
LINK         OD1 ASP D 334                CA    CA D 601     1555   1555  2.37  
LINK         OD2 ASP D 334                CA    CA D 601     1555   1555  2.36  
LINK         OE1 GLU D 336                CA    CA D 601     1555   1555  2.37  
LINK         OD1 ASP D 381                CA    CA D 601     1555   1555  2.37  
LINK         OD2 ASP D 381                CA    CA D 601     1555   1555  2.37  
LINK         O   VAL D 382                CA    CA D 601     1555   1555  2.39  
LINK         ND2 ASN D 422                 C1  NAG D 605     1555   1555  1.44  
LINK         ND2 ASN F 277                 C1  NAG F 602     1555   1555  1.43  
LINK         OD1 ASP F 334                CA    CA F 601     1555   1555  2.37  
LINK         OD2 ASP F 334                CA    CA F 601     1555   1555  2.36  
LINK         OE1 GLU F 336                CA    CA F 601     1555   1555  2.36  
LINK         OD1 ASP F 381                CA    CA F 601     1555   1555  2.36  
LINK         OD2 ASP F 381                CA    CA F 601     1555   1555  2.37  
LINK         O   VAL F 382                CA    CA F 601     1555   1555  2.39  
LINK         ND2 ASN F 422                 C1  NAG F 605     1555   1555  1.44  
LINK         ND2 ASN H 277                 C1  NAG H 602     1555   1555  1.44  
LINK         OD1 ASP H 334                CA    CA H 601     1555   1555  2.38  
LINK         OD2 ASP H 334                CA    CA H 601     1555   1555  2.36  
LINK         OE1 GLU H 336                CA    CA H 601     1555   1555  2.37  
LINK         OD1 ASP H 381                CA    CA H 601     1555   1555  2.37  
LINK         OD2 ASP H 381                CA    CA H 601     1555   1555  2.38  
LINK         O   VAL H 382                CA    CA H 601     1555   1555  2.39  
LINK         ND2 ASN H 422                 C1  NAG H 604     1555   1555  1.44  
LINK         ND2 ASN J 277                 C1  NAG J 602     1555   1555  1.45  
LINK         OD1 ASP J 334                CA    CA J 601     1555   1555  2.38  
LINK         OD2 ASP J 334                CA    CA J 601     1555   1555  2.36  
LINK         OE1 GLU J 336                CA    CA J 601     1555   1555  2.36  
LINK         OD1 ASP J 381                CA    CA J 601     1555   1555  2.37  
LINK         OD2 ASP J 381                CA    CA J 601     1555   1555  2.38  
LINK         O   VAL J 382                CA    CA J 601     1555   1555  2.38  
LINK         ND2 ASN J 422                 C1  NAG J 605     1555   1555  1.43  
LINK         ND2 ASN L 277                 C1  NAG L 602     1555   1555  1.44  
LINK         OD1 ASP L 334                CA    CA L 601     1555   1555  2.37  
LINK         OD2 ASP L 334                CA    CA L 601     1555   1555  2.36  
LINK         OE1 GLU L 336                CA    CA L 601     1555   1555  2.37  
LINK         OD1 ASP L 381                CA    CA L 601     1555   1555  2.36  
LINK         OD2 ASP L 381                CA    CA L 601     1555   1555  2.37  
LINK         O   VAL L 382                CA    CA L 601     1555   1555  2.39  
LINK         ND2 ASN L 422                 C1  NAG L 604     1555   1555  1.45  
LINK        CA    CA A 801                 O   HOH A 934     1555   1555  2.37  
LINK        CA    CA A 801                 O   HOH A 921     1555   1555  2.79  
LINK        CA    CA A 803                 O   HOH A 911     1555   1555  2.60  
LINK        CA    CA A 803                 O   HOH A 926     1555   1555  2.16  
LINK        CA    CA C 801                 O   HOH C 914     1555   1555  2.29  
LINK        CA    CA C 801                 O   HOH C 941     1555   1555  2.39  
LINK        CA    CA E 801                 O   HOH E 936     1555   1555  2.53  
LINK        CA    CA E 801                 O   HOH E 935     1555   1555  2.40  
LINK        CA    CA E 803                 O   HOH E 906     1555   1555  2.92  
LINK        CA    CA E 803                 O   HOH E 922     1555   1555  2.09  
LINK        CA    CA G 801                 O   HOH G 922     1555   1555  2.53  
LINK        CA    CA I 801                 O   HOH I 928     1555   1555  2.40  
LINK        CA    CA I 801                 O   HOH I 930     1555   1555  2.45  
LINK        CA    CA K 801                 O   HOH K 941     1555   1555  2.49  
LINK        CA    CA K 803                 O   HOH K 925     1555   1555  2.51  
LINK        CA    CA B 601                 O   HOH B 705     1555   1555  2.21  
LINK        CA    CA B 601                 O   HOH B 724     1555   1555  2.52  
LINK         O4  NAG B 602                 C1  NAG B 603     1555   1555  1.44  
LINK         C1  FUC B 604                 O6  NAG B 605     1555   1555  1.45  
LINK         O4  NAG B 605                 C1  NAG B 606     1555   1555  1.43  
LINK         O4  NAG B 606                 C1  BMA B 607     1555   1555  1.45  
LINK        CA    CA D 601                 O   HOH D 715     1555   1555  2.45  
LINK        CA    CA D 601                 O   HOH D 710     1555   1555  2.36  
LINK         O4  NAG D 602                 C1  NAG D 603     1555   1555  1.44  
LINK         C1  FUC D 604                 O6  NAG D 605     1555   1555  1.45  
LINK         O4  NAG D 605                 C1  NAG D 606     1555   1555  1.46  
LINK        CA    CA F 601                 O   HOH F 706     1555   1555  2.66  
LINK        CA    CA F 601                 O   HOH F 715     1555   1555  2.60  
LINK         O4  NAG F 602                 C1  NAG F 603     1555   1555  1.44  
LINK         C1  FUC F 604                 O6  NAG F 605     1555   1555  1.44  
LINK        CA    CA H 601                 O   HOH H 715     1555   1555  2.52  
LINK         C1  FUC H 603                 O6  NAG H 604     1555   1555  1.42  
LINK         O4  NAG H 604                 C1  NAG H 605     1555   1555  1.42  
LINK         O4  NAG H 605                 C1  BMA H 606     1555   1555  1.46  
LINK        CA    CA J 601                 O   HOH J 705     1555   1555  2.48  
LINK         O4  NAG J 602                 C1  NAG J 603     1555   1555  1.45  
LINK         C1  FUC J 604                 O6  NAG J 605     1555   1555  1.44  
LINK         O4  NAG J 605                 C1  NAG J 606     1555   1555  1.42  
LINK        CA    CA L 601                 O   HOH L 712     1555   1555  2.53  
LINK         C1  FUC L 603                 O6  NAG L 604     1555   1555  1.46  
LINK         O4  NAG L 604                 C1  NAG L 605     1555   1555  1.44  
CISPEP   1 THR B  390    PRO B  391          0         2.41                     
CISPEP   2 THR D  390    PRO D  391          0         2.24                     
CISPEP   3 THR F  390    PRO F  391          0         2.20                     
CISPEP   4 THR H  390    PRO H  391          0         2.05                     
CISPEP   5 THR J  390    PRO J  391          0         3.02                     
CISPEP   6 THR L  390    PRO L  391          0         2.02                     
SITE     1 AC1  6 GLU A 242  ASP A 325  CYS A 433  ASN A 436                    
SITE     2 AC1  6 HOH A 921  HOH A 934                                          
SITE     1 AC2  6 GLU A 446  ASN A 449  PHE A 451  GLU A 453                    
SITE     2 AC2  6 GLU A 456  ASP A 459                                          
SITE     1 AC3  7 ASP A 511  ILE A 512  GLU A 514  ASN A 526                    
SITE     2 AC3  7 ILE A 527  HOH A 911  HOH A 926                               
SITE     1 AC4  6 GLU C 242  ASP C 325  CYS C 433  ASN C 436                    
SITE     2 AC4  6 HOH C 914  HOH C 941                                          
SITE     1 AC5  6 GLU C 446  ASN C 449  PHE C 451  GLU C 453                    
SITE     2 AC5  6 GLU C 456  ASP C 459                                          
SITE     1 AC6  5 ASP C 511  ILE C 512  GLU C 514  ASN C 526                    
SITE     2 AC6  5 ILE C 527                                                     
SITE     1 AC7  6 GLU E 242  ASP E 325  CYS E 433  ASN E 436                    
SITE     2 AC7  6 HOH E 935  HOH E 936                                          
SITE     1 AC8  7 GLU E 446  CYS E 447  ASN E 449  PHE E 451                    
SITE     2 AC8  7 GLU E 453  GLU E 456  ASP E 459                               
SITE     1 AC9  7 ASP E 511  ILE E 512  GLU E 514  ASN E 526                    
SITE     2 AC9  7 ILE E 527  HOH E 906  HOH E 922                               
SITE     1 AD1  5 GLU G 242  ASP G 325  CYS G 433  ASN G 436                    
SITE     2 AD1  5 HOH G 922                                                     
SITE     1 AD2  6 GLU G 446  ASN G 449  PHE G 451  GLU G 453                    
SITE     2 AD2  6 GLU G 456  ASP G 459                                          
SITE     1 AD3  5 ASP G 511  ILE G 512  GLU G 514  ASN G 526                    
SITE     2 AD3  5 ILE G 527                                                     
SITE     1 AD4  6 GLU I 242  ASP I 325  CYS I 433  ASN I 436                    
SITE     2 AD4  6 HOH I 928  HOH I 930                                          
SITE     1 AD5  6 GLU I 446  ASN I 449  PHE I 451  GLU I 453                    
SITE     2 AD5  6 GLU I 456  ASP I 459                                          
SITE     1 AD6  5 ASP I 511  ILE I 512  GLU I 514  ASN I 526                    
SITE     2 AD6  5 ILE I 527                                                     
SITE     1 AD7  5 GLU K 242  ASP K 325  CYS K 433  ASN K 436                    
SITE     2 AD7  5 HOH K 941                                                     
SITE     1 AD8  6 GLU K 446  ASN K 449  PHE K 451  GLU K 453                    
SITE     2 AD8  6 GLU K 456  ASP K 459                                          
SITE     1 AD9  6 ASP K 511  ILE K 512  GLU K 514  ASN K 526                    
SITE     2 AD9  6 ILE K 527  HOH K 925                                          
SITE     1 AE1  6 ASP B 334  GLU B 336  ASP B 381  VAL B 382                    
SITE     2 AE1  6 HOH B 705  HOH B 724                                          
SITE     1 AE2  6 ASP D 334  GLU D 336  ASP D 381  VAL D 382                    
SITE     2 AE2  6 HOH D 710  HOH D 715                                          
SITE     1 AE3  6 ASP F 334  GLU F 336  ASP F 381  VAL F 382                    
SITE     2 AE3  6 HOH F 706  HOH F 715                                          
SITE     1 AE4  5 ASP H 334  GLU H 336  ASP H 381  VAL H 382                    
SITE     2 AE4  5 HOH H 715                                                     
SITE     1 AE5  5 ASP J 334  GLU J 336  ASP J 381  VAL J 382                    
SITE     2 AE5  5 HOH J 705                                                     
SITE     1 AE6  5 ASP L 334  GLU L 336  ASP L 381  VAL L 382                    
SITE     2 AE6  5 HOH L 712                                                     
SITE     1 AE7  7 TYR B 234  LYS B 259  ILE B 261  ASN B 274                    
SITE     2 AE7  7 ASN B 277  HOH B 714  HOH B 770                               
SITE     1 AE8  7 GLN B 412  ASN B 422  THR B 424  HOH B 717                    
SITE     2 AE8  7 GLN G 539  PRO G 659  GLN G 660                               
SITE     1 AE9  6 TYR D 234  LYS D 259  ILE D 261  ASN D 274                    
SITE     2 AE9  6 ASN D 277  HOH D 725                                          
SITE     1 AF1  5 GLN D 412  ASN D 422  THR D 424  GLN E 539                    
SITE     2 AF1  5 PRO E 659                                                     
SITE     1 AF2  3 LYS F 259  ASN F 274  ASN F 277                               
SITE     1 AF3  8 GLN C 660  GLN F 412  ASN F 422  GLN F 423                    
SITE     2 AF3  8 THR F 424  HOH F 701  HOH F 730  HOH F 732                    
SITE     1 AF4  4 LYS H 259  ASN H 274  ASN H 277  HOH H 721                    
SITE     1 AF5  7 PRO A 659  GLN A 660  GLN H 412  ASN H 422                    
SITE     2 AF5  7 THR H 424  HOH H 730  HOH H 752                               
SITE     1 AF6  5 LYS J 259  ILE J 261  ASN J 274  ASN J 277                    
SITE     2 AF6  5 HOH J 743                                                     
SITE     1 AF7  9 THR J 390  GLN J 412  ASN J 422  THR J 424                    
SITE     2 AF7  9 SER J 463  HOH J 732  VAL K 538  PRO K 659                    
SITE     3 AF7  9 GLN K 660                                                     
SITE     1 AF8  4 LYS L 259  ILE L 261  ASN L 277  HOH L 703                    
SITE     1 AF9  6 VAL I 538  PRO I 659  GLN L 412  ASN L 422                    
SITE     2 AF9  6 GLN L 423  THR L 424                                          
CRYST1   83.579   83.608  293.543  86.40  88.17  59.95 P 1           6          
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      0.011965 -0.006920 -0.000008        0.00000                         
SCALE2      0.000000  0.013817 -0.000748        0.00000                         
SCALE3      0.000000  0.000000  0.003413        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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