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Database: PDB
Entry: 4XLW
LinkDB: 4XLW
Original site: 4XLW 
HEADER    PROTEIN BINDING                         14-JAN-15   4XLW              
TITLE     COMPLEX OF NOTCH1 (EGF11-13) BOUND TO DELTA-LIKE 4 (N-EGF2)           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 SYNONYM: NOTCH 1;                                                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DELTA-LIKE PROTEIN;                                        
COMPND   8 CHAIN: B, D, F, H;                                                   
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: NOTCH1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PACGP67A;                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  11 ORGANISM_COMMON: RAT;                                                
SOURCE  12 ORGANISM_TAXID: 10116;                                               
SOURCE  13 GENE: DLL4, DLL4_PREDICTED, RCG_26804;                               
SOURCE  14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PACGP67A                                  
KEYWDS    GLYCOSYLATION, EGF DOMAINS, RECEPTOR-LIGAND COMPLEX, PROTEIN BINDING  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.C.LUCA,K.M.JUDE,K.C.GARCIA                                          
REVDAT   5   20-SEP-17 4XLW    1       SOURCE REMARK                            
REVDAT   4   10-JUN-15 4XLW    1       REMARK                                   
REVDAT   3   27-MAY-15 4XLW    1       REMARK                                   
REVDAT   2   11-MAR-15 4XLW    1       JRNL                                     
REVDAT   1   04-MAR-15 4XLW    0                                                
JRNL        AUTH   V.C.LUCA,K.M.JUDE,N.W.PIERCE,M.V.NACHURY,S.FISCHER,          
JRNL        AUTH 2 K.C.GARCIA                                                   
JRNL        TITL   STRUCTURAL BIOLOGY. STRUCTURAL BASIS FOR NOTCH1 ENGAGEMENT   
JRNL        TITL 2 OF DELTA-LIKE 4.                                             
JRNL        REF    SCIENCE                       V. 347   847 2015              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   25700513                                                     
JRNL        DOI    10.1126/SCIENCE.1261093                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.39 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV-1839                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 84.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 26865                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.260                           
REMARK   3   R VALUE            (WORKING SET) : 0.257                           
REMARK   3   FREE R VALUE                     : 0.310                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1330                            
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 84.0896 -  7.0527    0.98     2895   148  0.2096 0.2774        
REMARK   3     2  7.0527 -  5.5983    1.00     2887   154  0.2508 0.2844        
REMARK   3     3  5.5983 -  4.8907    1.00     2874   144  0.2148 0.2597        
REMARK   3     4  4.8907 -  4.4436    1.00     2858   149  0.2130 0.2938        
REMARK   3     5  4.4436 -  4.1251    0.99     2832   148  0.2561 0.3252        
REMARK   3     6  4.1251 -  3.8819    0.99     2830   151  0.2958 0.3110        
REMARK   3     7  3.8819 -  3.6875    0.99     2854   147  0.3278 0.3604        
REMARK   3     8  3.6875 -  3.5270    0.99     2799   152  0.3550 0.4003        
REMARK   3     9  3.5270 -  3.3912    0.95     2706   137  0.3925 0.4580        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.690            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.800           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 87.04                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 141.3                          
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      :  0.012          12251                                  
REMARK   3   ANGLE     :  0.719          16606                                  
REMARK   3   CHIRALITY :  0.031           1746                                  
REMARK   3   PLANARITY :  0.003           2179                                  
REMARK   3   DIHEDRAL  : 13.224           4448                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 26                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 26:95 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.059    6.324  146.284              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5851 T22:   1.0928                                     
REMARK   3      T33:   1.9271 T12:   0.3616                                     
REMARK   3      T13:   0.3677 T23:   0.1914                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8601 L22:   4.1695                                     
REMARK   3      L33:   2.7089 L12:  -4.1919                                     
REMARK   3      L13:  -3.2294 L23:   3.3925                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1288 S12:  -0.7765 S13:  -0.5925                       
REMARK   3      S21:   1.6057 S22:   0.4599 S23:   2.0424                       
REMARK   3      S31:   0.6607 S32:   0.3016 S33:  -0.3233                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 96:123 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):    5.635   -0.221  141.388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0451 T22:   0.9191                                     
REMARK   3      T33:   1.5934 T12:   0.1391                                     
REMARK   3      T13:   0.2335 T23:  -0.2042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9586 L22:   6.7877                                     
REMARK   3      L33:   8.4467 L12:  -5.1625                                     
REMARK   3      L13:  -0.7105 L23:   1.3872                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3604 S12:  -0.1219 S13:   0.6558                       
REMARK   3      S21:   1.5601 S22:   0.7461 S23:   2.4908                       
REMARK   3      S31:   0.2261 S32:  -0.1688 S33:  -0.1616                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 124:185 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):    5.241    1.494  146.382              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0087 T22:   0.8959                                     
REMARK   3      T33:   1.2049 T12:   0.4175                                     
REMARK   3      T13:   0.0108 T23:   0.2165                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4027 L22:   8.2939                                     
REMARK   3      L33:   4.1933 L12:  -1.4015                                     
REMARK   3      L13:  -2.0107 L23:   3.5012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.5332 S12:  -0.4333 S13:   0.0710                       
REMARK   3      S21:   2.8609 S22:   1.3050 S23:   1.4825                       
REMARK   3      S31:   0.3097 S32:   0.4014 S33:   0.1267                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 186:284 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   32.331  -49.929  138.165              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1420 T22:   0.9576                                     
REMARK   3      T33:   1.0635 T12:   0.2386                                     
REMARK   3      T13:  -0.2955 T23:   0.0110                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4674 L22:   9.6537                                     
REMARK   3      L33:   0.5798 L12:  -5.3389                                     
REMARK   3      L13:  -0.9342 L23:  -0.5478                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4515 S12:  -0.1252 S13:   0.2869                       
REMARK   3      S21:   0.3316 S22:   0.8505 S23:  -0.5511                       
REMARK   3      S31:   0.2147 S32:   0.0105 S33:  -0.4241                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 482:482 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   11.759  -14.876  185.281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1657 T22:   0.8531                                     
REMARK   3      T33:   0.6442 T12:   0.1444                                     
REMARK   3      T13:  -0.1618 T23:   0.0346                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0107 L22:   2.4839                                     
REMARK   3      L33:   3.5998 L12:   1.4061                                     
REMARK   3      L13:  -1.5329 L23:  -0.2234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3220 S12:  -0.2206 S13:   0.4895                       
REMARK   3      S21:  -2.1509 S22:   0.5079 S23:   0.7196                       
REMARK   3      S31:   0.0181 S32:  -0.0410 S33:  -0.1506                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 493:530 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):    5.105   28.735  176.999              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3812 T22:   1.0574                                     
REMARK   3      T33:   2.1055 T12:   0.1452                                     
REMARK   3      T13:   0.0242 T23:   0.2181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1862 L22:   8.9693                                     
REMARK   3      L33:   2.3162 L12:  -6.8122                                     
REMARK   3      L13:   3.2859 L23:  -4.4033                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0222 S12:  -0.5618 S13:   0.2239                       
REMARK   3      S21:  -1.0778 S22:   0.1186 S23:   0.8531                       
REMARK   3      S31:   0.7508 S32:   1.0762 S33:  -1.1668                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 26:76 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.054    6.485  204.815              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1550 T22:   1.1617                                     
REMARK   3      T33:   0.5321 T12:   0.2455                                     
REMARK   3      T13:   0.3682 T23:  -0.2374                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4573 L22:   2.6409                                     
REMARK   3      L33:   4.9733 L12:   0.6281                                     
REMARK   3      L13:  -2.1595 L23:   0.2775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0618 S12:   0.5629 S13:   0.1012                       
REMARK   3      S21:   0.3544 S22:  -0.6976 S23:   1.5798                       
REMARK   3      S31:  -1.1424 S32:  -0.3232 S33:  -0.3042                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 77:117 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.668   -3.529  205.101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6634 T22:   0.8277                                     
REMARK   3      T33:   1.1760 T12:   0.0233                                     
REMARK   3      T13:   0.2568 T23:   0.0821                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4203 L22:   5.8912                                     
REMARK   3      L33:   2.7381 L12:  -3.7299                                     
REMARK   3      L13:  -1.1224 L23:   3.5175                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0045 S12:  -0.3307 S13:  -0.5707                       
REMARK   3      S21:   0.4470 S22:   0.4090 S23:   1.4050                       
REMARK   3      S31:   0.6772 S32:   0.0685 S33:  -0.2800                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 118:185 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.403    0.391  206.200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4880 T22:   0.8372                                     
REMARK   3      T33:   0.3716 T12:  -0.0016                                     
REMARK   3      T13:   0.3161 T23:  -0.0446                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3270 L22:   8.8260                                     
REMARK   3      L33:   3.4466 L12:  -2.0757                                     
REMARK   3      L13:   0.5323 L23:   1.9446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7784 S12:  -0.5551 S13:   0.0145                       
REMARK   3      S21:   0.0835 S22:   0.3008 S23:  -1.2263                       
REMARK   3      S31:  -0.4998 S32:  -0.0241 S33:   0.0506                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 186:283 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   24.075  -51.679  199.174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5035 T22:   0.9590                                     
REMARK   3      T33:   1.1988 T12:   0.2365                                     
REMARK   3      T13:  -0.2272 T23:   0.0398                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1481 L22:   4.9433                                     
REMARK   3      L33:  -0.0033 L12:  -2.8276                                     
REMARK   3      L13:  -0.6463 L23:   0.2469                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1203 S12:  -0.1374 S13:  -0.6967                       
REMARK   3      S21:   0.6413 S22:   0.4410 S23:   0.7547                       
REMARK   3      S31:   0.2085 S32:   0.1176 S33:  -0.3302                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: ( CHAIN F AND RESID 26:148 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):   16.683   23.645  143.445              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4071 T22:   1.0635                                     
REMARK   3      T33:   1.1378 T12:   0.1975                                     
REMARK   3      T13:  -0.4300 T23:  -0.0418                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1839 L22:   9.0094                                     
REMARK   3      L33:   2.3459 L12:  -0.7644                                     
REMARK   3      L13:   1.3593 L23:  -0.9896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0769 S12:   0.0129 S13:   0.3966                       
REMARK   3      S21:   1.4965 S22:   0.0712 S23:  -0.5576                       
REMARK   3      S31:  -0.0228 S32:   0.6272 S33:  -0.1910                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: ( CHAIN F AND RESID 149:213 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):    2.901   43.691  145.310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5045 T22:   1.2306                                     
REMARK   3      T33:   1.8804 T12:   0.3402                                     
REMARK   3      T13:  -0.3016 T23:  -0.1640                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0359 L22:   2.9029                                     
REMARK   3      L33:   3.2905 L12:  -0.8703                                     
REMARK   3      L13:   1.6826 L23:  -1.3990                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6103 S12:  -0.3862 S13:   0.7093                       
REMARK   3      S21:   1.7140 S22:   0.4572 S23:   1.4673                       
REMARK   3      S31:  -0.4349 S32:   0.2761 S33:   0.2731                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: ( CHAIN F AND RESID 214:255 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -14.292   78.526  139.592              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9692 T22:   1.2443                                     
REMARK   3      T33:   2.5013 T12:   0.4801                                     
REMARK   3      T13:  -0.0604 T23:  -0.1866                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1054 L22:   7.0629                                     
REMARK   3      L33:   3.7999 L12:  -4.0514                                     
REMARK   3      L13:   0.7293 L23:  -4.1336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6342 S12:  -0.2074 S13:  -0.1748                       
REMARK   3      S21:   2.3101 S22:  -0.1930 S23:   2.2410                       
REMARK   3      S31:  -1.1910 S32:  -0.1859 S33:   0.7916                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: ( CHAIN F AND RESID 256:283 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -30.565   98.871  134.334              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5437 T22:   1.0782                                     
REMARK   3      T33:   2.3450 T12:   0.2668                                     
REMARK   3      T13:   0.2007 T23:   0.0805                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7404 L22:   2.9381                                     
REMARK   3      L33:   3.1185 L12:   0.8321                                     
REMARK   3      L13:   1.4057 L23:  -2.0806                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3885 S12:   1.2137 S13:  -0.6835                       
REMARK   3      S21:   0.0501 S22:  -1.3036 S23:  -2.0651                       
REMARK   3      S31:   0.6039 S32:   0.0817 S33:   0.8176                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: ( CHAIN H AND RESID 26:48 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):    9.562   19.679  209.386              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7501 T22:   0.8660                                     
REMARK   3      T33:   0.7992 T12:  -0.0322                                     
REMARK   3      T13:  -0.4560 T23:  -0.1452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8989 L22:   8.1741                                     
REMARK   3      L33:   4.2019 L12:  -3.3630                                     
REMARK   3      L13:  -0.1783 L23:  -4.2994                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3946 S12:   0.1224 S13:   0.0975                       
REMARK   3      S21:   1.8835 S22:   0.4398 S23:   1.2027                       
REMARK   3      S31:  -0.6149 S32:   0.1751 S33:  -0.0621                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: ( CHAIN H AND RESID 49:95 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):    9.648   20.692  204.096              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6912 T22:   0.5829                                     
REMARK   3      T33:   0.7040 T12:   0.0205                                     
REMARK   3      T13:   0.1687 T23:  -0.0756                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2233 L22:   8.7590                                     
REMARK   3      L33:   8.2528 L12:  -3.9889                                     
REMARK   3      L13:   1.1239 L23:  -2.7008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6011 S12:   0.2338 S13:   0.8743                       
REMARK   3      S21:  -0.2263 S22:  -0.3039 S23:  -0.2848                       
REMARK   3      S31:  -0.5417 S32:   0.1849 S33:  -0.2878                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: ( CHAIN H AND RESID 96:117 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):    1.135   30.642  200.722              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2628 T22:   0.9432                                     
REMARK   3      T33:   1.3659 T12:   0.1787                                     
REMARK   3      T13:  -0.3738 T23:   0.3835                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9554 L22:   4.2561                                     
REMARK   3      L33:   5.4438 L12:   4.9601                                     
REMARK   3      L13:   0.8608 L23:   2.2607                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7262 S12:  -0.4368 S13:  -0.0357                       
REMARK   3      S21:   1.5997 S22:  -0.1222 S23:   0.6193                       
REMARK   3      S31:  -0.2102 S32:  -0.3283 S33:  -0.7136                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: ( CHAIN H AND RESID 118:185 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):    5.124   24.439  206.107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0501 T22:   0.6592                                     
REMARK   3      T33:   0.7538 T12:   0.0103                                     
REMARK   3      T13:  -0.2113 T23:  -0.0501                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2926 L22:   6.4824                                     
REMARK   3      L33:   3.2698 L12:  -3.8372                                     
REMARK   3      L13:   3.3320 L23:  -2.9167                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5411 S12:  -0.3094 S13:   1.2949                       
REMARK   3      S21:  -0.1149 S22:   0.1456 S23:  -0.1016                       
REMARK   3      S31:  -0.5167 S32:  -0.3331 S33:   0.2996                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: ( CHAIN H AND RESID 186:234 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.840   62.947  201.416              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6175 T22:   1.1023                                     
REMARK   3      T33:   1.3100 T12:   0.3984                                     
REMARK   3      T13:  -0.1152 T23:  -0.1506                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8264 L22:   5.5507                                     
REMARK   3      L33:   1.3946 L12:   0.4440                                     
REMARK   3      L13:  -1.6340 L23:  -0.0767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3854 S12:  -0.0892 S13:  -0.5114                       
REMARK   3      S21:   1.2213 S22:   0.7330 S23:   0.4813                       
REMARK   3      S31:  -0.3473 S32:  -0.1524 S33:  -1.0862                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: ( CHAIN H AND RESID 236:283 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -31.896   91.490  198.024              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4117 T22:   0.8732                                     
REMARK   3      T33:   1.6536 T12:   0.2396                                     
REMARK   3      T13:   0.2097 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3366 L22:   5.2907                                     
REMARK   3      L33:   5.3756 L12:  -1.7552                                     
REMARK   3      L13:   4.0025 L23:  -3.4035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1276 S12:  -0.5200 S13:  -0.4401                       
REMARK   3      S21:   0.9339 S22:   1.1331 S23:   0.2082                       
REMARK   3      S31:   0.1716 S32:  -0.2982 S33:  -0.0183                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 414:492 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   18.692  -13.084  124.938              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4075 T22:   0.9779                                     
REMARK   3      T33:   1.5774 T12:   0.1639                                     
REMARK   3      T13:  -0.2641 T23:   0.2641                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9507 L22:   7.8534                                     
REMARK   3      L33:   3.3037 L12:  -0.3949                                     
REMARK   3      L13:  -0.9918 L23:  -1.5330                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5319 S12:   0.3708 S13:   0.9470                       
REMARK   3      S21:  -2.4494 S22:  -0.3702 S23:   0.0941                       
REMARK   3      S31:   0.1018 S32:   0.2344 S33:  -0.1645                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 493:526 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   13.397   23.041  117.053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.4958 T22:   1.3405                                     
REMARK   3      T33:   1.7437 T12:   0.2639                                     
REMARK   3      T13:   0.2109 T23:   0.4695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1206 L22:   3.0805                                     
REMARK   3      L33:   0.0240 L12:   2.9881                                     
REMARK   3      L13:   0.2796 L23:   0.0481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2183 S12:   0.5648 S13:   1.9312                       
REMARK   3      S21:  -1.1843 S22:  -1.0106 S23:  -0.8613                       
REMARK   3      S31:  -0.6197 S32:   0.9745 S33:   0.9524                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: ( CHAIN E AND RESID 414:492 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.358   41.661  125.354              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4704 T22:   1.0596                                     
REMARK   3      T33:   2.8016 T12:   0.2800                                     
REMARK   3      T13:  -0.3829 T23:   0.0694                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1706 L22:   3.6531                                     
REMARK   3      L33:   2.5760 L12:   1.2504                                     
REMARK   3      L13:   0.4194 L23:   0.6643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7344 S12:   0.4805 S13:  -0.1162                       
REMARK   3      S21:  -1.1133 S22:  -0.9466 S23:   0.1498                       
REMARK   3      S31:  -0.3500 S32:   0.0022 S33:   0.1446                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: ( CHAIN E AND RESID 493:530 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):    2.971   -1.863  116.686              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6468 T22:   1.0564                                     
REMARK   3      T33:   1.7493 T12:   0.1584                                     
REMARK   3      T13:  -0.0604 T23:   0.1578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6003 L22:   7.2498                                     
REMARK   3      L33:   3.3143 L12:  -2.4074                                     
REMARK   3      L13:  -0.2807 L23:   4.7377                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8954 S12:  -0.4437 S13:   0.8662                       
REMARK   3      S21:  -1.7245 S22:   0.5982 S23:   1.4253                       
REMARK   3      S31:  -1.6943 S32:  -1.0862 S33:   0.2762                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: ( CHAIN G AND RESID 414:492 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -10.038   40.221  185.614              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8723 T22:   0.7657                                     
REMARK   3      T33:   1.3345 T12:   0.1192                                     
REMARK   3      T13:   0.0276 T23:  -0.1486                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7838 L22:   4.3851                                     
REMARK   3      L33:   4.8020 L12:  -2.4207                                     
REMARK   3      L13:   1.2973 L23:   0.4707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5995 S12:   0.3881 S13:   0.3116                       
REMARK   3      S21:  -1.5465 S22:  -0.4303 S23:   0.5792                       
REMARK   3      S31:  -0.0790 S32:   0.1947 S33:  -0.1345                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: ( CHAIN G AND RESID 493:530 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.037   -3.079  176.189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9368 T22:   1.0696                                     
REMARK   3      T33:   1.2744 T12:   0.2620                                     
REMARK   3      T13:  -0.1300 T23:  -0.1362                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0666 L22:   4.5535                                     
REMARK   3      L33:   0.3243 L12:  -6.0816                                     
REMARK   3      L13:  -1.2568 L23:   0.9494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3333 S12:  -0.5307 S13:   0.1473                       
REMARK   3      S21:  -0.8721 S22:  -0.0711 S23:  -1.7570                       
REMARK   3      S31:  -0.4796 S32:  -1.3294 S33:  -0.2942                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 2189                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN E                                     
REMARK   3     ATOM PAIRS NUMBER  : 2189                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN G                                     
REMARK   3     ATOM PAIRS NUMBER  : 2189                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 4803                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B                                     
REMARK   3     SELECTION          : CHAIN F                                     
REMARK   3     ATOM PAIRS NUMBER  : 4803                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B                                     
REMARK   3     SELECTION          : CHAIN H                                     
REMARK   3     ATOM PAIRS NUMBER  : 4803                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4XLW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000205873.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999956                           
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27009                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.390                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 84.064                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.21700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.1200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.39                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.22000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.190                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MGSO4, TRIS-HCL P, D-(+)       
REMARK 280  -GALACTOSE, PH 8.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.78500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL                          
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL                          
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL                          
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL                          
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 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     ASP A   412                                                      
REMARK 465     VAL A   413                                                      
REMARK 465     SER A   527                                                      
REMARK 465     GLY A   528                                                      
REMARK 465     ARG A   529                                                      
REMARK 465     LEU A   530                                                      
REMARK 465     GLU A   531                                                      
REMARK 465     VAL A   532                                                      
REMARK 465     LEU A   533                                                      
REMARK 465     PHE A   534                                                      
REMARK 465     GLN A   535                                                      
REMARK 465     GLY B    97                                                      
REMARK 465     SER B    98                                                      
REMARK 465     ALA B   285                                                      
REMARK 465     ALA B   286                                                      
REMARK 465     ASP C   412                                                      
REMARK 465     VAL C   413                                                      
REMARK 465     VAL C   532                                                      
REMARK 465     LEU C   533                                                      
REMARK 465     PHE C   534                                                      
REMARK 465     GLN C   535                                                      
REMARK 465     GLY D    97                                                      
REMARK 465     SER D    98                                                      
REMARK 465     ALA D   286                                                      
REMARK 465     ASP E   412                                                      
REMARK 465     VAL E   413                                                      
REMARK 465     GLU E   531                                                      
REMARK 465     VAL E   532                                                      
REMARK 465     LEU E   533                                                      
REMARK 465     PHE E   534                                                      
REMARK 465     GLN E   535                                                      
REMARK 465     GLY F    97                                                      
REMARK 465     SER F    98                                                      
REMARK 465     ALA F   285                                                      
REMARK 465     ALA F   286                                                      
REMARK 465     ASP G   412                                                      
REMARK 465     VAL G   413                                                      
REMARK 465     GLU G   531                                                      
REMARK 465     VAL G   532                                                      
REMARK 465     LEU G   533                                                      
REMARK 465     PHE G   534                                                      
REMARK 465     GLN G   535                                                      
REMARK 465     GLY H    97                                                      
REMARK 465     SER H    98                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A 515    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 518    CG   CD   CE   NZ                                   
REMARK 470     GLU B  71    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 515    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 518    CG   CD   CE   NZ                                   
REMARK 470     GLN E 515    CG   CD   OE1  NE2                                  
REMARK 470     LYS E 518    CG   CD   CE   NZ                                   
REMARK 470     GLN G 515    CG   CD   OE1  NE2                                  
REMARK 470     LYS G 518    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU C   511     O3   NAG H   301              1.26            
REMARK 500   OE2  GLU A   511     O3   NAG F   301              1.26            
REMARK 500   OE1  GLU E   493     OD1  ASP E   507              1.33            
REMARK 500   OE1  GLU A   493     OD1  ASP A   507              1.34            
REMARK 500   OE1  GLU G   493     OD1  ASP G   507              1.46            
REMARK 500   OE1  GLU C   493     OD1  ASP C   507              1.46            
REMARK 500   OD1  ASN A   431     O    THR A   432              1.78            
REMARK 500   CD   GLU C   511     O3   NAG H   301              2.07            
REMARK 500   O    TYR F    65     O4   FUC E   904              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 418       40.49    -77.26                                   
REMARK 500    ALA A 420     -170.40    -68.49                                   
REMARK 500    LYS A 508     -110.93   -129.03                                   
REMARK 500    CYS A 525       72.43     51.63                                   
REMARK 500    ARG B  41      -28.72     66.31                                   
REMARK 500    ASN B  87     -111.39     57.32                                   
REMARK 500    ARG B 130       73.36     55.40                                   
REMARK 500    ILE B 140      -68.59    -97.79                                   
REMARK 500    ASP B 192       52.93   -150.97                                   
REMARK 500    ASP B 193     -158.47   -141.42                                   
REMARK 500    THR B 263     -169.51   -116.74                                   
REMARK 500    CYS B 281       78.39     53.70                                   
REMARK 500    ASP B 282       22.96   -153.24                                   
REMARK 500    LEU C 418       40.43    -77.26                                   
REMARK 500    ALA C 420     -170.17    -68.58                                   
REMARK 500    SER C 435     -159.79   -154.03                                   
REMARK 500    LYS C 508     -110.73   -129.00                                   
REMARK 500    CYS C 525       73.07     52.17                                   
REMARK 500    GLN C 526       17.21   -143.94                                   
REMARK 500    SER C 527     -158.02    -84.82                                   
REMARK 500    ARG C 529      168.72     60.20                                   
REMARK 500    ARG D  41      -28.97     66.27                                   
REMARK 500    ASN D  87     -111.43     57.53                                   
REMARK 500    ARG D 100      108.15    -60.00                                   
REMARK 500    ARG D 130       74.33     55.48                                   
REMARK 500    ILE D 140      -68.44    -96.88                                   
REMARK 500    ASP D 192       52.99   -150.66                                   
REMARK 500    ASP D 193     -159.46   -141.72                                   
REMARK 500    CYS D 281       78.86     53.86                                   
REMARK 500    ASP D 282       22.95   -152.74                                   
REMARK 500    LEU E 418       40.51    -77.03                                   
REMARK 500    ALA E 420     -170.61    -68.59                                   
REMARK 500    SER E 435     -158.69   -159.26                                   
REMARK 500    LYS E 508     -111.00   -128.05                                   
REMARK 500    CYS E 525       70.94     51.85                                   
REMARK 500    ARG E 529       77.08   -165.42                                   
REMARK 500    ARG F  41      -28.58     67.35                                   
REMARK 500    ASN F  87     -111.92     57.86                                   
REMARK 500    ARG F 100      108.07    -56.53                                   
REMARK 500    ARG F 130       73.83     54.88                                   
REMARK 500    ILE F 140      -68.69    -97.67                                   
REMARK 500    ASP F 192       52.12   -150.48                                   
REMARK 500    ASP F 193     -158.98   -142.71                                   
REMARK 500    CYS F 281       77.02     53.52                                   
REMARK 500    ASP F 282       23.73   -154.86                                   
REMARK 500    LEU G 418       40.58    -76.80                                   
REMARK 500    ALA G 420     -169.87    -68.62                                   
REMARK 500    SER G 435     -158.02   -159.11                                   
REMARK 500    LYS G 508     -110.42   -129.75                                   
REMARK 500    CYS G 525       72.62     52.21                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 414   OD2                                                    
REMARK 620 2 GLU A 415   OE1  60.6                                              
REMARK 620 3 ASN A 431   OD1  56.1  77.1                                        
REMARK 620 4 THR A 432   O    87.8 116.4  41.2                                  
REMARK 620 5 LEU A 433   O   147.4 127.0 150.0 109.6                            
REMARK 620 6 SER A 435   O   102.4  60.7  65.1  77.2 108.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 452   OD1                                                    
REMARK 620 2 ASP A 452   OD2  52.5                                              
REMARK 620 3 VAL A 453   O    73.2 109.7                                        
REMARK 620 4 GLU A 455   OE1 115.1 167.3  60.2                                  
REMARK 620 5 ASP A 469   OD1 146.9 133.5  75.2  54.3                            
REMARK 620 6 ASP A 469   OD2 126.7  81.0 105.5 108.3  54.3                      
REMARK 620 7 GLN A 470   O   116.6 115.6 128.0  70.9  90.8 105.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 603  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 490   OD1                                                    
REMARK 620 2 THR A 491   O    88.7                                              
REMARK 620 3 GLU A 493   OE1 163.0  75.7                                        
REMARK 620 4 GLU A 493   OE2 112.5  64.8  54.8                                  
REMARK 620 5 ASP A 507   OD1 150.7  78.6  32.6  85.9                            
REMARK 620 6 ASP A 507   OD2 112.0 117.7  81.8 135.5  54.5                      
REMARK 620 7 LYS A 508   O    92.5 168.9 101.6 104.7 105.1  72.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 605  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 414   OD2                                                    
REMARK 620 2 GLU C 415   OE1  82.5                                              
REMARK 620 3 ASN C 431   OD1  64.6  97.1                                        
REMARK 620 4 THR C 432   O   112.3 134.6  57.9                                  
REMARK 620 5 SER C 435   O   117.7  75.9  61.3  59.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 606  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 452   OD1                                                    
REMARK 620 2 ASP C 452   OD2  53.5                                              
REMARK 620 3 VAL C 453   O    72.2 109.4                                        
REMARK 620 4 GLU C 455   OE1 115.3 167.9  59.7                                  
REMARK 620 5 ASP C 469   OD1 144.3 131.4  74.1  53.6                            
REMARK 620 6 ASP C 469   OD2 126.8  79.9 106.7 107.4  54.3                      
REMARK 620 7 GLN C 470   O   116.0 118.0 125.0  69.6  92.9 107.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 607  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C 490   OD1                                                    
REMARK 620 2 THR C 491   O    88.9                                              
REMARK 620 3 GLU C 493   OE1 161.9  74.2                                        
REMARK 620 4 GLU C 493   OE2 112.0  63.6  54.7                                  
REMARK 620 5 ASP C 507   OD1 148.0  78.9  35.8  89.1                            
REMARK 620 6 ASP C 507   OD2 109.3 117.9  85.0 138.7  54.2                      
REMARK 620 7 LYS C 508   O    93.0 169.9 102.4 106.6 104.0  70.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 901  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 452   OD1                                                    
REMARK 620 2 ASP E 452   OD2  53.7                                              
REMARK 620 3 VAL E 453   O    71.8 109.1                                        
REMARK 620 4 GLU E 455   OE1 115.2 167.7  59.5                                  
REMARK 620 5 ASP E 469   OD1 141.6 129.3  72.4  54.5                            
REMARK 620 6 ASP E 469   OD2 125.7  78.6 106.8 108.2  54.5                      
REMARK 620 7 GLN E 470   O   115.5 120.6 122.1  67.5  95.2 110.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 902  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN E 490   OD1                                                    
REMARK 620 2 THR E 491   O    75.4                                              
REMARK 620 3 GLU E 493   OE1 144.9  69.6                                        
REMARK 620 4 GLU E 493   OE2 105.3  59.4  54.8                                  
REMARK 620 5 ASP E 507   OD1 131.4  68.0  31.7  82.6                            
REMARK 620 6 ASP E 507   OD2 103.1  95.6  82.1 134.7  52.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 901  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 452   OD1                                                    
REMARK 620 2 ASP G 452   OD2  53.4                                              
REMARK 620 3 VAL G 453   O    70.2 109.5                                        
REMARK 620 4 GLU G 455   OE1 113.2 166.5  60.6                                  
REMARK 620 5 ASP G 469   OD1 144.9 131.2  77.3  58.3                            
REMARK 620 6 ASP G 469   OD2 128.9  80.7 113.1 111.1  54.2                      
REMARK 620 7 GLN G 470   O   111.3 116.7 121.1  66.7  96.6 108.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 902  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN G 490   OD1                                                    
REMARK 620 2 THR G 491   O    88.0                                              
REMARK 620 3 GLU G 493   OE1 159.5  77.3                                        
REMARK 620 4 GLU G 493   OE2 105.9  64.3  54.9                                  
REMARK 620 5 ASP G 507   OD1 155.0  80.4  35.9  88.9                            
REMARK 620 6 ASP G 507   OD2 116.3 120.4  83.7 137.4  54.4                      
REMARK 620 7 LYS G 508   O    91.1 163.8  99.1 100.5 106.1  74.3                
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 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC A 606 bound   
REMARK 800  to SER A 435                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC A 604 bound   
REMARK 800  to SER A 458                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide FUC A 605 bound   
REMARK 800  to THR A 466                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC A 607 bound   
REMARK 800  to SER A 496                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 301 bound   
REMARK 800  to ASN B 161                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC C 603 bound   
REMARK 800  to SER C 435                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC C 601 bound   
REMARK 800  to SER C 458                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide FUC C 602 bound   
REMARK 800  to THR C 466                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC C 604 bound   
REMARK 800  to SER C 496                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 301 bound   
REMARK 800  to ASN D 161                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC E 905 bound   
REMARK 800  to SER E 435                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC E 903 bound   
REMARK 800  to SER E 458                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide FUC E 904 bound   
REMARK 800  to THR E 466                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC E 906 bound   
REMARK 800  to SER E 496                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG F 301 bound   
REMARK 800  to ASN F 78                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG F 302 bound   
REMARK 800  to ASN F 161                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC G 905 bound   
REMARK 800  to SER G 435                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC G 903 bound   
REMARK 800  to SER G 458                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide FUC G 904 bound   
REMARK 800  to THR G 466                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC G 906 bound   
REMARK 800  to SER G 496                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG H 301 bound   
REMARK 800  to ASN H 78                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG H 302 bound   
REMARK 800  to ASN H 161                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4XL1   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 DELTA-LIKE PROTEIN HAD C-TERMINAL TAG CDQAAAHHHHHHHH WHICH IS        
REMARK 999 EITHER DISORDERED OR CLEAVED AFTER TREATMENT WITH CARBOXYPEPTIDASE   
REMARK 999 PRIOR TO CRYSTALLIZATION.                                            
DBREF  4XLW A  412   526  UNP    Q07008   NOTC1_RAT      412    526             
DBREF  4XLW B   27   283  UNP    D3ZHH1   D3ZHH1_RAT      27    283             
DBREF  4XLW C  412   526  UNP    Q07008   NOTC1_RAT      412    526             
DBREF  4XLW D   27   283  UNP    D3ZHH1   D3ZHH1_RAT      27    283             
DBREF  4XLW E  412   526  UNP    Q07008   NOTC1_RAT      412    526             
DBREF  4XLW F   27   283  UNP    D3ZHH1   D3ZHH1_RAT      27    283             
DBREF  4XLW G  412   526  UNP    Q07008   NOTC1_RAT      412    526             
DBREF  4XLW H   27   283  UNP    D3ZHH1   D3ZHH1_RAT      27    283             
SEQADV 4XLW SER A  527  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLY A  528  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW ARG A  529  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW LEU A  530  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLU A  531  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW VAL A  532  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW LEU A  533  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW PHE A  534  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLN A  535  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW SER B   26  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW SER B   28  UNP  D3ZHH1    GLY    28 ENGINEERED MUTATION            
SEQADV 4XLW LEU B  107  UNP  D3ZHH1    PHE   107 ENGINEERED MUTATION            
SEQADV 4XLW PRO B  206  UNP  D3ZHH1    LEU   206 ENGINEERED MUTATION            
SEQADV 4XLW LYS B  257  UNP  D3ZHH1    ASN   257 ENGINEERED MUTATION            
SEQADV 4XLW ALA B  284  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW ALA B  285  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW ALA B  286  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW SER C  527  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLY C  528  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW ARG C  529  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW LEU C  530  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLU C  531  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW VAL C  532  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW LEU C  533  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW PHE C  534  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLN C  535  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW SER D   26  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW SER D   28  UNP  D3ZHH1    GLY    28 ENGINEERED MUTATION            
SEQADV 4XLW LEU D  107  UNP  D3ZHH1    PHE   107 ENGINEERED MUTATION            
SEQADV 4XLW PRO D  206  UNP  D3ZHH1    LEU   206 ENGINEERED MUTATION            
SEQADV 4XLW LYS D  257  UNP  D3ZHH1    ASN   257 ENGINEERED MUTATION            
SEQADV 4XLW ALA D  284  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW ALA D  285  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW ALA D  286  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW SER E  527  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLY E  528  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW ARG E  529  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW LEU E  530  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLU E  531  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW VAL E  532  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW LEU E  533  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW PHE E  534  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLN E  535  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW SER F   26  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW SER F   28  UNP  D3ZHH1    GLY    28 ENGINEERED MUTATION            
SEQADV 4XLW LEU F  107  UNP  D3ZHH1    PHE   107 ENGINEERED MUTATION            
SEQADV 4XLW PRO F  206  UNP  D3ZHH1    LEU   206 ENGINEERED MUTATION            
SEQADV 4XLW LYS F  257  UNP  D3ZHH1    ASN   257 ENGINEERED MUTATION            
SEQADV 4XLW ALA F  284  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW ALA F  285  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW ALA F  286  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW SER G  527  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLY G  528  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW ARG G  529  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW LEU G  530  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLU G  531  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW VAL G  532  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW LEU G  533  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW PHE G  534  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW GLN G  535  UNP  Q07008              EXPRESSION TAG                 
SEQADV 4XLW SER H   26  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW SER H   28  UNP  D3ZHH1    GLY    28 ENGINEERED MUTATION            
SEQADV 4XLW LEU H  107  UNP  D3ZHH1    PHE   107 ENGINEERED MUTATION            
SEQADV 4XLW PRO H  206  UNP  D3ZHH1    LEU   206 ENGINEERED MUTATION            
SEQADV 4XLW LYS H  257  UNP  D3ZHH1    ASN   257 ENGINEERED MUTATION            
SEQADV 4XLW ALA H  284  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW ALA H  285  UNP  D3ZHH1              EXPRESSION TAG                 
SEQADV 4XLW ALA H  286  UNP  D3ZHH1              EXPRESSION TAG                 
SEQRES   1 A  124  ASP VAL ASP GLU CYS ALA LEU GLY ALA ASN PRO CYS GLU          
SEQRES   2 A  124  HIS ALA GLY LYS CYS LEU ASN THR LEU GLY SER PHE GLU          
SEQRES   3 A  124  CYS GLN CYS LEU GLN GLY TYR THR GLY PRO ARG CYS GLU          
SEQRES   4 A  124  ILE ASP VAL ASN GLU CYS ILE SER ASN PRO CYS GLN ASN          
SEQRES   5 A  124  ASP ALA THR CYS LEU ASP GLN ILE GLY GLU PHE GLN CYS          
SEQRES   6 A  124  ILE CYS MET PRO GLY TYR GLU GLY VAL TYR CYS GLU ILE          
SEQRES   7 A  124  ASN THR ASP GLU CYS ALA SER SER PRO CYS LEU HIS ASN          
SEQRES   8 A  124  GLY ARG CYS VAL ASP LYS ILE ASN GLU PHE LEU CYS GLN          
SEQRES   9 A  124  CYS PRO LYS GLY PHE SER GLY HIS LEU CYS GLN SER GLY          
SEQRES  10 A  124  ARG LEU GLU VAL LEU PHE GLN                                  
SEQRES   1 B  261  SER SER SER ILE PHE GLN LEU ARG LEU GLN GLU PHE ALA          
SEQRES   2 B  261  ASN GLU ARG GLY MET LEU ALA ASN GLY ARG PRO CYS GLU          
SEQRES   3 B  261  PRO GLY CYS ARG THR PHE PHE ARG ILE CYS LEU LYS HIS          
SEQRES   4 B  261  TYR GLN ALA THR PHE SER GLU GLY PRO CYS THR PHE GLY          
SEQRES   5 B  261  ASN VAL SER THR PRO VAL LEU GLY THR ASN SER PHE VAL          
SEQRES   6 B  261  ILE ARG ASP LYS ASN SER GLY SER GLY ARG ASN PRO LEU          
SEQRES   7 B  261  GLN LEU PRO LEU ASN PHE THR TRP PRO GLY THR PHE SER          
SEQRES   8 B  261  LEU ASN ILE GLN ALA TRP HIS THR PRO GLY ASP ASP LEU          
SEQRES   9 B  261  ARG PRO GLU THR SER PRO GLY ASN SER LEU ILE SER GLN          
SEQRES  10 B  261  ILE ILE ILE GLN GLY SER LEU ALA VAL GLY MLY ASN TRP          
SEQRES  11 B  261  LYS SER ASP GLU GLN ASN ASN THR LEU THR ARG LEU ARG          
SEQRES  12 B  261  TYR SER TYR ARG VAL VAL CYS SER ASP ASN TYR TYR GLY          
SEQRES  13 B  261  ASP SER CYS SER ARG LEU CYS MLY MLY ARG ASP ASP HIS          
SEQRES  14 B  261  PHE GLY HIS TYR GLU CYS GLN PRO ASP GLY SER PRO SER          
SEQRES  15 B  261  CYS LEU PRO GLY TRP THR GLY MLY TYR CYS ASP GLN PRO          
SEQRES  16 B  261  ILE CYS LEU SER GLY CYS HIS GLU GLN ASN GLY TYR CYS          
SEQRES  17 B  261  SER MLY PRO ASP GLU CYS ASN CYS ARG PRO GLY TRP GLN          
SEQRES  18 B  261  GLY PRO LEU CYS ASN GLU CYS ILE PRO HIS LYS GLY CYS          
SEQRES  19 B  261  ARG HIS GLY THR CYS THR ILE PRO TRP GLN CYS ALA CYS          
SEQRES  20 B  261  ASP GLU GLY TRP GLY GLY LEU PHE CYS ASP GLN ALA ALA          
SEQRES  21 B  261  ALA                                                          
SEQRES   1 C  124  ASP VAL ASP GLU CYS ALA LEU GLY ALA ASN PRO CYS GLU          
SEQRES   2 C  124  HIS ALA GLY LYS CYS LEU ASN THR LEU GLY SER PHE GLU          
SEQRES   3 C  124  CYS GLN CYS LEU GLN GLY TYR THR GLY PRO ARG CYS GLU          
SEQRES   4 C  124  ILE ASP VAL ASN GLU CYS ILE SER ASN PRO CYS GLN ASN          
SEQRES   5 C  124  ASP ALA THR CYS LEU ASP GLN ILE GLY GLU PHE GLN CYS          
SEQRES   6 C  124  ILE CYS MET PRO GLY TYR GLU GLY VAL TYR CYS GLU ILE          
SEQRES   7 C  124  ASN THR ASP GLU CYS ALA SER SER PRO CYS LEU HIS ASN          
SEQRES   8 C  124  GLY ARG CYS VAL ASP LYS ILE ASN GLU PHE LEU CYS GLN          
SEQRES   9 C  124  CYS PRO LYS GLY PHE SER GLY HIS LEU CYS GLN SER GLY          
SEQRES  10 C  124  ARG LEU GLU VAL LEU PHE GLN                                  
SEQRES   1 D  261  SER SER SER ILE PHE GLN LEU ARG LEU GLN GLU PHE ALA          
SEQRES   2 D  261  ASN GLU ARG GLY MET LEU ALA ASN GLY ARG PRO CYS GLU          
SEQRES   3 D  261  PRO GLY CYS ARG THR PHE PHE ARG ILE CYS LEU LYS HIS          
SEQRES   4 D  261  TYR GLN ALA THR PHE SER GLU GLY PRO CYS THR PHE GLY          
SEQRES   5 D  261  ASN VAL SER THR PRO VAL LEU GLY THR ASN SER PHE VAL          
SEQRES   6 D  261  ILE ARG ASP LYS ASN SER GLY SER GLY ARG ASN PRO LEU          
SEQRES   7 D  261  GLN LEU PRO LEU ASN PHE THR TRP PRO GLY THR PHE SER          
SEQRES   8 D  261  LEU ASN ILE GLN ALA TRP HIS THR PRO GLY ASP ASP LEU          
SEQRES   9 D  261  ARG PRO GLU THR SER PRO GLY ASN SER LEU ILE SER GLN          
SEQRES  10 D  261  ILE ILE ILE GLN GLY SER LEU ALA VAL GLY MLY ASN TRP          
SEQRES  11 D  261  LYS SER ASP GLU GLN ASN ASN THR LEU THR ARG LEU ARG          
SEQRES  12 D  261  TYR SER TYR ARG VAL VAL CYS SER ASP ASN TYR TYR GLY          
SEQRES  13 D  261  ASP SER CYS SER ARG LEU CYS MLY MLY ARG ASP ASP HIS          
SEQRES  14 D  261  PHE GLY HIS TYR GLU CYS GLN PRO ASP GLY SER PRO SER          
SEQRES  15 D  261  CYS LEU PRO GLY TRP THR GLY MLY TYR CYS ASP GLN PRO          
SEQRES  16 D  261  ILE CYS LEU SER GLY CYS HIS GLU GLN ASN GLY TYR CYS          
SEQRES  17 D  261  SER MLY PRO ASP GLU CYS ASN CYS ARG PRO GLY TRP GLN          
SEQRES  18 D  261  GLY PRO LEU CYS ASN GLU CYS ILE PRO HIS LYS GLY CYS          
SEQRES  19 D  261  ARG HIS GLY THR CYS THR ILE PRO TRP GLN CYS ALA CYS          
SEQRES  20 D  261  ASP GLU GLY TRP GLY GLY LEU PHE CYS ASP GLN ALA ALA          
SEQRES  21 D  261  ALA                                                          
SEQRES   1 E  124  ASP VAL ASP GLU CYS ALA LEU GLY ALA ASN PRO CYS GLU          
SEQRES   2 E  124  HIS ALA GLY LYS CYS LEU ASN THR LEU GLY SER PHE GLU          
SEQRES   3 E  124  CYS GLN CYS LEU GLN GLY TYR THR GLY PRO ARG CYS GLU          
SEQRES   4 E  124  ILE ASP VAL ASN GLU CYS ILE SER ASN PRO CYS GLN ASN          
SEQRES   5 E  124  ASP ALA THR CYS LEU ASP GLN ILE GLY GLU PHE GLN CYS          
SEQRES   6 E  124  ILE CYS MET PRO GLY TYR GLU GLY VAL TYR CYS GLU ILE          
SEQRES   7 E  124  ASN THR ASP GLU CYS ALA SER SER PRO CYS LEU HIS ASN          
SEQRES   8 E  124  GLY ARG CYS VAL ASP LYS ILE ASN GLU PHE LEU CYS GLN          
SEQRES   9 E  124  CYS PRO LYS GLY PHE SER GLY HIS LEU CYS GLN SER GLY          
SEQRES  10 E  124  ARG LEU GLU VAL LEU PHE GLN                                  
SEQRES   1 F  261  SER SER SER ILE PHE GLN LEU ARG LEU GLN GLU PHE ALA          
SEQRES   2 F  261  ASN GLU ARG GLY MET LEU ALA ASN GLY ARG PRO CYS GLU          
SEQRES   3 F  261  PRO GLY CYS ARG THR PHE PHE ARG ILE CYS LEU LYS HIS          
SEQRES   4 F  261  TYR GLN ALA THR PHE SER GLU GLY PRO CYS THR PHE GLY          
SEQRES   5 F  261  ASN VAL SER THR PRO VAL LEU GLY THR ASN SER PHE VAL          
SEQRES   6 F  261  ILE ARG ASP LYS ASN SER GLY SER GLY ARG ASN PRO LEU          
SEQRES   7 F  261  GLN LEU PRO LEU ASN PHE THR TRP PRO GLY THR PHE SER          
SEQRES   8 F  261  LEU ASN ILE GLN ALA TRP HIS THR PRO GLY ASP ASP LEU          
SEQRES   9 F  261  ARG PRO GLU THR SER PRO GLY ASN SER LEU ILE SER GLN          
SEQRES  10 F  261  ILE ILE ILE GLN GLY SER LEU ALA VAL GLY MLY ASN TRP          
SEQRES  11 F  261  LYS SER ASP GLU GLN ASN ASN THR LEU THR ARG LEU ARG          
SEQRES  12 F  261  TYR SER TYR ARG VAL VAL CYS SER ASP ASN TYR TYR GLY          
SEQRES  13 F  261  ASP SER CYS SER ARG LEU CYS MLY MLY ARG ASP ASP HIS          
SEQRES  14 F  261  PHE GLY HIS TYR GLU CYS GLN PRO ASP GLY SER PRO SER          
SEQRES  15 F  261  CYS LEU PRO GLY TRP THR GLY MLY TYR CYS ASP GLN PRO          
SEQRES  16 F  261  ILE CYS LEU SER GLY CYS HIS GLU GLN ASN GLY TYR CYS          
SEQRES  17 F  261  SER MLY PRO ASP GLU CYS ASN CYS ARG PRO GLY TRP GLN          
SEQRES  18 F  261  GLY PRO LEU CYS ASN GLU CYS ILE PRO HIS LYS GLY CYS          
SEQRES  19 F  261  ARG HIS GLY THR CYS THR ILE PRO TRP GLN CYS ALA CYS          
SEQRES  20 F  261  ASP GLU GLY TRP GLY GLY LEU PHE CYS ASP GLN ALA ALA          
SEQRES  21 F  261  ALA                                                          
SEQRES   1 G  124  ASP VAL ASP GLU CYS ALA LEU GLY ALA ASN PRO CYS GLU          
SEQRES   2 G  124  HIS ALA GLY LYS CYS LEU ASN THR LEU GLY SER PHE GLU          
SEQRES   3 G  124  CYS GLN CYS LEU GLN GLY TYR THR GLY PRO ARG CYS GLU          
SEQRES   4 G  124  ILE ASP VAL ASN GLU CYS ILE SER ASN PRO CYS GLN ASN          
SEQRES   5 G  124  ASP ALA THR CYS LEU ASP GLN ILE GLY GLU PHE GLN CYS          
SEQRES   6 G  124  ILE CYS MET PRO GLY TYR GLU GLY VAL TYR CYS GLU ILE          
SEQRES   7 G  124  ASN THR ASP GLU CYS ALA SER SER PRO CYS LEU HIS ASN          
SEQRES   8 G  124  GLY ARG CYS VAL ASP LYS ILE ASN GLU PHE LEU CYS GLN          
SEQRES   9 G  124  CYS PRO LYS GLY PHE SER GLY HIS LEU CYS GLN SER GLY          
SEQRES  10 G  124  ARG LEU GLU VAL LEU PHE GLN                                  
SEQRES   1 H  261  SER SER SER ILE PHE GLN LEU ARG LEU GLN GLU PHE ALA          
SEQRES   2 H  261  ASN GLU ARG GLY MET LEU ALA ASN GLY ARG PRO CYS GLU          
SEQRES   3 H  261  PRO GLY CYS ARG THR PHE PHE ARG ILE CYS LEU LYS HIS          
SEQRES   4 H  261  TYR GLN ALA THR PHE SER GLU GLY PRO CYS THR PHE GLY          
SEQRES   5 H  261  ASN VAL SER THR PRO VAL LEU GLY THR ASN SER PHE VAL          
SEQRES   6 H  261  ILE ARG ASP LYS ASN SER GLY SER GLY ARG ASN PRO LEU          
SEQRES   7 H  261  GLN LEU PRO LEU ASN PHE THR TRP PRO GLY THR PHE SER          
SEQRES   8 H  261  LEU ASN ILE GLN ALA TRP HIS THR PRO GLY ASP ASP LEU          
SEQRES   9 H  261  ARG PRO GLU THR SER PRO GLY ASN SER LEU ILE SER GLN          
SEQRES  10 H  261  ILE ILE ILE GLN GLY SER LEU ALA VAL GLY MLY ASN TRP          
SEQRES  11 H  261  LYS SER ASP GLU GLN ASN ASN THR LEU THR ARG LEU ARG          
SEQRES  12 H  261  TYR SER TYR ARG VAL VAL CYS SER ASP ASN TYR TYR GLY          
SEQRES  13 H  261  ASP SER CYS SER ARG LEU CYS MLY MLY ARG ASP ASP HIS          
SEQRES  14 H  261  PHE GLY HIS TYR GLU CYS GLN PRO ASP GLY SER PRO SER          
SEQRES  15 H  261  CYS LEU PRO GLY TRP THR GLY MLY TYR CYS ASP GLN PRO          
SEQRES  16 H  261  ILE CYS LEU SER GLY CYS HIS GLU GLN ASN GLY TYR CYS          
SEQRES  17 H  261  SER MLY PRO ASP GLU CYS ASN CYS ARG PRO GLY TRP GLN          
SEQRES  18 H  261  GLY PRO LEU CYS ASN GLU CYS ILE PRO HIS LYS GLY CYS          
SEQRES  19 H  261  ARG HIS GLY THR CYS THR ILE PRO TRP GLN CYS ALA CYS          
SEQRES  20 H  261  ASP GLU GLY TRP GLY GLY LEU PHE CYS ASP GLN ALA ALA          
SEQRES  21 H  261  ALA                                                          
MODRES 4XLW MLY B  153  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY B  189  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY B  190  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY B  215  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY B  235  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY D  153  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY D  189  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY D  190  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY D  215  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY D  235  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY F  153  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY F  189  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY F  190  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY F  215  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY F  235  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY H  153  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY H  189  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY H  190  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY H  215  LYS  MODIFIED RESIDUE                                   
MODRES 4XLW MLY H  235  LYS  MODIFIED RESIDUE                                   
HET    MLY  B 153      11                                                       
HET    MLY  B 189      11                                                       
HET    MLY  B 190      11                                                       
HET    MLY  B 215      11                                                       
HET    MLY  B 235      11                                                       
HET    MLY  D 153      11                                                       
HET    MLY  D 189      11                                                       
HET    MLY  D 190      11                                                       
HET    MLY  D 215      11                                                       
HET    MLY  D 235      11                                                       
HET    MLY  F 153      11                                                       
HET    MLY  F 189      11                                                       
HET    MLY  F 190      11                                                       
HET    MLY  F 215      11                                                       
HET    MLY  F 235      11                                                       
HET    MLY  H 153      11                                                       
HET    MLY  H 189      11                                                       
HET    MLY  H 190      11                                                       
HET    MLY  H 215      11                                                       
HET    MLY  H 235      11                                                       
HET     CA  A 601       1                                                       
HET     CA  A 602       1                                                       
HET     CA  A 603       1                                                       
HET    BGC  A 604      11                                                       
HET    FUC  A 605      10                                                       
HET    BGC  A 606      11                                                       
HET    BGC  A 607      11                                                       
HET    NAG  B 301      14                                                       
HET    BGC  C 601      11                                                       
HET    FUC  C 602      10                                                       
HET    BGC  C 603      11                                                       
HET    BGC  C 604      11                                                       
HET     CA  C 605       1                                                       
HET     CA  C 606       1                                                       
HET     CA  C 607       1                                                       
HET    NAG  D 301      14                                                       
HET     CA  E 901       1                                                       
HET     CA  E 902       1                                                       
HET    BGC  E 903      11                                                       
HET    FUC  E 904      10                                                       
HET    BGC  E 905      11                                                       
HET    BGC  E 906      11                                                       
HET    NAG  F 301      14                                                       
HET    NAG  F 302      14                                                       
HET     CA  G 901       1                                                       
HET     CA  G 902       1                                                       
HET    BGC  G 903      11                                                       
HET    FUC  G 904      10                                                       
HET    BGC  G 905      11                                                       
HET    BGC  G 906      11                                                       
HET    NAG  H 301      14                                                       
HET    NAG  H 302      14                                                       
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM      CA CALCIUM ION                                                      
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   2  MLY    20(C8 H18 N2 O2)                                             
FORMUL   9   CA    10(CA 2+)                                                    
FORMUL  12  BGC    12(C6 H12 O6)                                                
FORMUL  13  FUC    4(C6 H12 O5)                                                 
FORMUL  16  NAG    6(C8 H15 N O6)                                               
HELIX    1 AA1 ASP A  414  LEU A  418  5                                   5    
HELIX    2 AA2 ASP C  414  LEU C  418  5                                   5    
HELIX    3 AA3 ASP E  414  LEU E  418  5                                   5    
HELIX    4 AA4 ASP G  414  LEU G  418  5                                   5    
SHEET    1 AA1 2 LYS A 428  ASN A 431  0                                        
SHEET    2 AA1 2 PHE A 436  GLN A 439 -1  O  GLN A 439   N  LYS A 428           
SHEET    1 AA2 2 TYR A 444  THR A 445  0                                        
SHEET    2 AA2 2 ILE A 451  ASP A 452 -1  O  ILE A 451   N  THR A 445           
SHEET    1 AA3 2 THR A 466  ASP A 469  0                                        
SHEET    2 AA3 2 PHE A 474  ILE A 477 -1  O  GLN A 475   N  LEU A 468           
SHEET    1 AA4 2 TYR A 482  GLU A 483  0                                        
SHEET    2 AA4 2 ILE A 489  ASN A 490 -1  O  ILE A 489   N  GLU A 483           
SHEET    1 AA5 2 ARG A 504  ASP A 507  0                                        
SHEET    2 AA5 2 PHE A 512  GLN A 515 -1  O  LEU A 513   N  VAL A 506           
SHEET    1 AA6 8 PHE B  89  VAL B  90  0                                        
SHEET    2 AA6 8 SER B  28  ALA B  38 -1  N  PHE B  37   O  PHE B  89           
SHEET    3 AA6 8 ARG B 166  CYS B 175 -1  O  SER B 170   N  ARG B  33           
SHEET    4 AA6 8 LYS B 156  ASN B 162 -1  N  LYS B 156   O  TYR B 171           
SHEET    5 AA6 8 LYS F 156  ASN F 162 -1  O  ASN F 161   N  ASN B 161           
SHEET    6 AA6 8 ARG F 166  CYS F 175 -1  O  LEU F 167   N  GLN F 160           
SHEET    7 AA6 8 SER F  28  ALA F  38 -1  N  ILE F  29   O  VAL F 174           
SHEET    8 AA6 8 PHE F  89  VAL F  90 -1  O  PHE F  89   N  PHE F  37           
SHEET    1 AA7 8 LEU B 103  PRO B 106  0                                        
SHEET    2 AA7 8 SER B  28  ALA B  38 -1  N  LEU B  32   O  LEU B 103           
SHEET    3 AA7 8 ARG B 166  CYS B 175 -1  O  SER B 170   N  ARG B  33           
SHEET    4 AA7 8 LYS B 156  ASN B 162 -1  N  LYS B 156   O  TYR B 171           
SHEET    5 AA7 8 LYS F 156  ASN F 162 -1  O  ASN F 161   N  ASN B 161           
SHEET    6 AA7 8 ARG F 166  CYS F 175 -1  O  LEU F 167   N  GLN F 160           
SHEET    7 AA7 8 SER F  28  ALA F  38 -1  N  ILE F  29   O  VAL F 174           
SHEET    8 AA7 8 LEU F 103  PRO F 106 -1  O  LEU F 103   N  LEU F  32           
SHEET    1 AA8 3 GLY B  77  SER B  80  0                                        
SHEET    2 AA8 3 ARG B  55  LYS B  63 -1  N  ILE B  60   O  VAL B  79           
SHEET    3 AA8 3 GLY B  85  THR B  86 -1  O  GLY B  85   N  THR B  56           
SHEET    1 AA9 4 GLY B  77  SER B  80  0                                        
SHEET    2 AA9 4 ARG B  55  LYS B  63 -1  N  ILE B  60   O  VAL B  79           
SHEET    3 AA9 4 THR B 114  HIS B 123 -1  O  ASN B 118   N  CYS B  61           
SHEET    4 AA9 4 SER B 138  SER B 148 -1  O  SER B 141   N  ALA B 121           
SHEET    1 AB1 2 TYR B 179  TYR B 180  0                                        
SHEET    2 AB1 2 ARG B 186  LEU B 187 -1  O  ARG B 186   N  TYR B 180           
SHEET    1 AB2 3 ARG B 191  ASP B 193  0                                        
SHEET    2 AB2 3 GLY B 196  CYS B 200 -1  O  GLY B 196   N  ASP B 193           
SHEET    3 AB2 3 PRO B 206  CYS B 208 -1  O  SER B 207   N  GLU B 199           
SHEET    1 AB3 2 TRP B 212  THR B 213  0                                        
SHEET    2 AB3 2 GLN B 219  PRO B 220 -1  O  GLN B 219   N  THR B 213           
SHEET    1 AB4 2 GLY B 231  TYR B 232  0                                        
SHEET    2 AB4 2 ASN B 240  CYS B 241 -1  O  ASN B 240   N  TYR B 232           
SHEET    1 AB5 2 TRP B 245  GLN B 246  0                                        
SHEET    2 AB5 2 GLU B 252  CYS B 253 -1  O  GLU B 252   N  GLN B 246           
SHEET    1 AB6 2 GLY B 262  THR B 263  0                                        
SHEET    2 AB6 2 ALA B 271  CYS B 272 -1  O  ALA B 271   N  THR B 263           
SHEET    1 AB7 2 LYS C 428  THR C 432  0                                        
SHEET    2 AB7 2 SER C 435  GLN C 439 -1  O  GLN C 439   N  LYS C 428           
SHEET    1 AB8 2 TYR C 444  THR C 445  0                                        
SHEET    2 AB8 2 ILE C 451  ASP C 452 -1  O  ILE C 451   N  THR C 445           
SHEET    1 AB9 2 THR C 466  ASP C 469  0                                        
SHEET    2 AB9 2 PHE C 474  ILE C 477 -1  O  GLN C 475   N  LEU C 468           
SHEET    1 AC1 2 TYR C 482  GLU C 483  0                                        
SHEET    2 AC1 2 ILE C 489  ASN C 490 -1  O  ILE C 489   N  GLU C 483           
SHEET    1 AC2 2 ARG C 504  ASP C 507  0                                        
SHEET    2 AC2 2 PHE C 512  GLN C 515 -1  O  LEU C 513   N  VAL C 506           
SHEET    1 AC3 8 PHE D  89  VAL D  90  0                                        
SHEET    2 AC3 8 SER D  28  ALA D  38 -1  N  PHE D  37   O  PHE D  89           
SHEET    3 AC3 8 ARG D 166  CYS D 175 -1  O  SER D 170   N  ARG D  33           
SHEET    4 AC3 8 LYS D 156  ASN D 162 -1  N  GLN D 160   O  LEU D 167           
SHEET    5 AC3 8 LYS H 156  ASN H 162 -1  O  ASN H 161   N  ASN D 161           
SHEET    6 AC3 8 ARG H 166  CYS H 175 -1  O  LEU H 167   N  GLN H 160           
SHEET    7 AC3 8 SER H  28  ALA H  38 -1  N  ARG H  33   O  SER H 170           
SHEET    8 AC3 8 PHE H  89  VAL H  90 -1  O  PHE H  89   N  PHE H  37           
SHEET    1 AC4 8 LEU D 103  PRO D 106  0                                        
SHEET    2 AC4 8 SER D  28  ALA D  38 -1  N  LEU D  32   O  LEU D 103           
SHEET    3 AC4 8 ARG D 166  CYS D 175 -1  O  SER D 170   N  ARG D  33           
SHEET    4 AC4 8 LYS D 156  ASN D 162 -1  N  GLN D 160   O  LEU D 167           
SHEET    5 AC4 8 LYS H 156  ASN H 162 -1  O  ASN H 161   N  ASN D 161           
SHEET    6 AC4 8 ARG H 166  CYS H 175 -1  O  LEU H 167   N  GLN H 160           
SHEET    7 AC4 8 SER H  28  ALA H  38 -1  N  ARG H  33   O  SER H 170           
SHEET    8 AC4 8 LEU H 103  LEU H 107 -1  O  LEU H 103   N  LEU H  32           
SHEET    1 AC5 3 GLY D  77  SER D  80  0                                        
SHEET    2 AC5 3 ARG D  55  LYS D  63 -1  N  ILE D  60   O  VAL D  79           
SHEET    3 AC5 3 GLY D  85  THR D  86 -1  O  GLY D  85   N  THR D  56           
SHEET    1 AC6 4 GLY D  77  SER D  80  0                                        
SHEET    2 AC6 4 ARG D  55  LYS D  63 -1  N  ILE D  60   O  VAL D  79           
SHEET    3 AC6 4 THR D 114  HIS D 123 -1  O  SER D 116   N  LYS D  63           
SHEET    4 AC6 4 SER D 138  SER D 148 -1  O  SER D 141   N  ALA D 121           
SHEET    1 AC7 2 TYR D 179  TYR D 180  0                                        
SHEET    2 AC7 2 ARG D 186  LEU D 187 -1  O  ARG D 186   N  TYR D 180           
SHEET    1 AC8 3 ARG D 191  ASP D 193  0                                        
SHEET    2 AC8 3 GLY D 196  CYS D 200 -1  O  GLY D 196   N  ASP D 193           
SHEET    3 AC8 3 PRO D 206  CYS D 208 -1  O  SER D 207   N  GLU D 199           
SHEET    1 AC9 2 TRP D 212  THR D 213  0                                        
SHEET    2 AC9 2 GLN D 219  PRO D 220 -1  O  GLN D 219   N  THR D 213           
SHEET    1 AD1 2 GLY D 231  TYR D 232  0                                        
SHEET    2 AD1 2 ASN D 240  CYS D 241 -1  O  ASN D 240   N  TYR D 232           
SHEET    1 AD2 2 TRP D 245  GLN D 246  0                                        
SHEET    2 AD2 2 GLU D 252  CYS D 253 -1  O  GLU D 252   N  GLN D 246           
SHEET    1 AD3 2 GLY D 262  THR D 263  0                                        
SHEET    2 AD3 2 ALA D 271  CYS D 272 -1  O  ALA D 271   N  THR D 263           
SHEET    1 AD4 2 LYS E 428  THR E 432  0                                        
SHEET    2 AD4 2 SER E 435  GLN E 439 -1  O  GLN E 439   N  LYS E 428           
SHEET    1 AD5 2 TYR E 444  THR E 445  0                                        
SHEET    2 AD5 2 ILE E 451  ASP E 452 -1  O  ILE E 451   N  THR E 445           
SHEET    1 AD6 2 THR E 466  ASP E 469  0                                        
SHEET    2 AD6 2 PHE E 474  ILE E 477 -1  O  GLN E 475   N  LEU E 468           
SHEET    1 AD7 2 TYR E 482  GLU E 483  0                                        
SHEET    2 AD7 2 ILE E 489  ASN E 490 -1  O  ILE E 489   N  GLU E 483           
SHEET    1 AD8 2 ARG E 504  ASP E 507  0                                        
SHEET    2 AD8 2 PHE E 512  GLN E 515 -1  O  LEU E 513   N  VAL E 506           
SHEET    1 AD9 2 PHE E 520  SER E 521  0                                        
SHEET    2 AD9 2 SER E 527  GLY E 528 -1  O  SER E 527   N  SER E 521           
SHEET    1 AE1 3 GLY F  77  SER F  80  0                                        
SHEET    2 AE1 3 ARG F  55  LYS F  63 -1  N  ILE F  60   O  VAL F  79           
SHEET    3 AE1 3 GLY F  85  THR F  86 -1  O  GLY F  85   N  THR F  56           
SHEET    1 AE2 4 GLY F  77  SER F  80  0                                        
SHEET    2 AE2 4 ARG F  55  LYS F  63 -1  N  ILE F  60   O  VAL F  79           
SHEET    3 AE2 4 THR F 114  HIS F 123 -1  O  ASN F 118   N  CYS F  61           
SHEET    4 AE2 4 SER F 138  SER F 148 -1  O  SER F 141   N  ALA F 121           
SHEET    1 AE3 2 TYR F 179  TYR F 180  0                                        
SHEET    2 AE3 2 ARG F 186  LEU F 187 -1  O  ARG F 186   N  TYR F 180           
SHEET    1 AE4 3 ARG F 191  ASP F 193  0                                        
SHEET    2 AE4 3 GLY F 196  CYS F 200 -1  O  GLY F 196   N  ASP F 193           
SHEET    3 AE4 3 PRO F 206  CYS F 208 -1  O  SER F 207   N  GLU F 199           
SHEET    1 AE5 2 TRP F 212  THR F 213  0                                        
SHEET    2 AE5 2 GLN F 219  PRO F 220 -1  O  GLN F 219   N  THR F 213           
SHEET    1 AE6 2 GLY F 231  TYR F 232  0                                        
SHEET    2 AE6 2 ASN F 240  CYS F 241 -1  O  ASN F 240   N  TYR F 232           
SHEET    1 AE7 2 TRP F 245  GLN F 246  0                                        
SHEET    2 AE7 2 GLU F 252  CYS F 253 -1  O  GLU F 252   N  GLN F 246           
SHEET    1 AE8 2 GLY F 262  THR F 263  0                                        
SHEET    2 AE8 2 ALA F 271  CYS F 272 -1  O  ALA F 271   N  THR F 263           
SHEET    1 AE9 2 LYS G 428  THR G 432  0                                        
SHEET    2 AE9 2 SER G 435  GLN G 439 -1  O  GLN G 439   N  LYS G 428           
SHEET    1 AF1 2 TYR G 444  THR G 445  0                                        
SHEET    2 AF1 2 ILE G 451  ASP G 452 -1  O  ILE G 451   N  THR G 445           
SHEET    1 AF2 2 THR G 466  ASP G 469  0                                        
SHEET    2 AF2 2 PHE G 474  ILE G 477 -1  O  GLN G 475   N  LEU G 468           
SHEET    1 AF3 2 TYR G 482  GLU G 483  0                                        
SHEET    2 AF3 2 ILE G 489  ASN G 490 -1  O  ILE G 489   N  GLU G 483           
SHEET    1 AF4 2 ARG G 504  ASP G 507  0                                        
SHEET    2 AF4 2 PHE G 512  GLN G 515 -1  O  GLN G 515   N  ARG G 504           
SHEET    1 AF5 2 PHE G 520  SER G 521  0                                        
SHEET    2 AF5 2 SER G 527  GLY G 528 -1  O  SER G 527   N  SER G 521           
SHEET    1 AF6 3 GLY H  77  SER H  80  0                                        
SHEET    2 AF6 3 ARG H  55  LYS H  63 -1  N  ILE H  60   O  VAL H  79           
SHEET    3 AF6 3 GLY H  85  THR H  86 -1  O  GLY H  85   N  THR H  56           
SHEET    1 AF7 4 GLY H  77  SER H  80  0                                        
SHEET    2 AF7 4 ARG H  55  LYS H  63 -1  N  ILE H  60   O  VAL H  79           
SHEET    3 AF7 4 THR H 114  HIS H 123 -1  O  TRP H 122   N  PHE H  57           
SHEET    4 AF7 4 SER H 138  SER H 148 -1  O  SER H 141   N  ALA H 121           
SHEET    1 AF8 2 TYR H 179  TYR H 180  0                                        
SHEET    2 AF8 2 ARG H 186  LEU H 187 -1  O  ARG H 186   N  TYR H 180           
SHEET    1 AF9 3 ARG H 191  ASP H 193  0                                        
SHEET    2 AF9 3 GLY H 196  CYS H 200 -1  O  GLY H 196   N  ASP H 193           
SHEET    3 AF9 3 PRO H 206  CYS H 208 -1  O  SER H 207   N  GLU H 199           
SHEET    1 AG1 2 TRP H 212  THR H 213  0                                        
SHEET    2 AG1 2 GLN H 219  PRO H 220 -1  O  GLN H 219   N  THR H 213           
SHEET    1 AG2 2 GLY H 231  TYR H 232  0                                        
SHEET    2 AG2 2 ASN H 240  CYS H 241 -1  O  ASN H 240   N  TYR H 232           
SHEET    1 AG3 2 TRP H 245  GLN H 246  0                                        
SHEET    2 AG3 2 GLU H 252  CYS H 253 -1  O  GLU H 252   N  GLN H 246           
SHEET    1 AG4 2 GLY H 262  THR H 263  0                                        
SHEET    2 AG4 2 ALA H 271  CYS H 272 -1  O  ALA H 271   N  THR H 263           
SSBOND   1 CYS A  416    CYS A  429                          1555   1555  2.04  
SSBOND   2 CYS A  423    CYS A  438                          1555   1555  2.03  
SSBOND   3 CYS A  440    CYS A  449                          1555   1555  2.03  
SSBOND   4 CYS A  456    CYS A  467                          1555   1555  2.03  
SSBOND   5 CYS A  461    CYS A  476                          1555   1555  2.03  
SSBOND   6 CYS A  478    CYS A  487                          1555   1555  2.03  
SSBOND   7 CYS A  494    CYS A  505                          1555   1555  2.03  
SSBOND   8 CYS A  499    CYS A  514                          1555   1555  2.03  
SSBOND   9 CYS A  516    CYS A  525                          1555   1555  2.03  
SSBOND  10 CYS B   50    CYS B   54                          1555   1555  2.03  
SSBOND  11 CYS B   61    CYS B   74                          1555   1555  2.03  
SSBOND  12 CYS B  175    CYS B  184                          1555   1555  2.03  
SSBOND  13 CYS B  188    CYS B  200                          1555   1555  2.03  
SSBOND  14 CYS B  208    CYS B  217                          1555   1555  2.03  
SSBOND  15 CYS B  222    CYS B  233                          1555   1555  2.03  
SSBOND  16 CYS B  226    CYS B  239                          1555   1555  2.04  
SSBOND  17 CYS B  241    CYS B  250                          1555   1555  2.03  
SSBOND  18 CYS B  253    CYS B  264                          1555   1555  2.04  
SSBOND  19 CYS B  259    CYS B  270                          1555   1555  2.03  
SSBOND  20 CYS B  272    CYS B  281                          1555   1555  2.03  
SSBOND  21 CYS C  416    CYS C  429                          1555   1555  2.04  
SSBOND  22 CYS C  423    CYS C  438                          1555   1555  2.03  
SSBOND  23 CYS C  440    CYS C  449                          1555   1555  2.03  
SSBOND  24 CYS C  456    CYS C  467                          1555   1555  2.03  
SSBOND  25 CYS C  461    CYS C  476                          1555   1555  2.03  
SSBOND  26 CYS C  478    CYS C  487                          1555   1555  2.03  
SSBOND  27 CYS C  494    CYS C  505                          1555   1555  2.03  
SSBOND  28 CYS C  499    CYS C  514                          1555   1555  2.03  
SSBOND  29 CYS C  516    CYS C  525                          1555   1555  2.03  
SSBOND  30 CYS D   50    CYS D   54                          1555   1555  2.03  
SSBOND  31 CYS D   61    CYS D   74                          1555   1555  2.03  
SSBOND  32 CYS D  175    CYS D  184                          1555   1555  2.03  
SSBOND  33 CYS D  188    CYS D  200                          1555   1555  2.03  
SSBOND  34 CYS D  208    CYS D  217                          1555   1555  2.03  
SSBOND  35 CYS D  222    CYS D  233                          1555   1555  2.03  
SSBOND  36 CYS D  226    CYS D  239                          1555   1555  2.03  
SSBOND  37 CYS D  241    CYS D  250                          1555   1555  2.03  
SSBOND  38 CYS D  253    CYS D  264                          1555   1555  2.04  
SSBOND  39 CYS D  259    CYS D  270                          1555   1555  2.03  
SSBOND  40 CYS D  272    CYS D  281                          1555   1555  2.03  
SSBOND  41 CYS E  416    CYS E  429                          1555   1555  2.03  
SSBOND  42 CYS E  423    CYS E  438                          1555   1555  2.03  
SSBOND  43 CYS E  440    CYS E  449                          1555   1555  2.03  
SSBOND  44 CYS E  456    CYS E  467                          1555   1555  2.03  
SSBOND  45 CYS E  461    CYS E  476                          1555   1555  2.02  
SSBOND  46 CYS E  478    CYS E  487                          1555   1555  2.03  
SSBOND  47 CYS E  494    CYS E  505                          1555   1555  2.03  
SSBOND  48 CYS E  499    CYS E  514                          1555   1555  2.03  
SSBOND  49 CYS E  516    CYS E  525                          1555   1555  2.03  
SSBOND  50 CYS F   50    CYS F   54                          1555   1555  2.03  
SSBOND  51 CYS F   61    CYS F   74                          1555   1555  2.03  
SSBOND  52 CYS F  175    CYS F  184                          1555   1555  2.03  
SSBOND  53 CYS F  188    CYS F  200                          1555   1555  2.03  
SSBOND  54 CYS F  208    CYS F  217                          1555   1555  2.03  
SSBOND  55 CYS F  222    CYS F  233                          1555   1555  2.03  
SSBOND  56 CYS F  226    CYS F  239                          1555   1555  2.03  
SSBOND  57 CYS F  241    CYS F  250                          1555   1555  2.03  
SSBOND  58 CYS F  253    CYS F  264                          1555   1555  2.04  
SSBOND  59 CYS F  259    CYS F  270                          1555   1555  2.03  
SSBOND  60 CYS F  272    CYS F  281                          1555   1555  2.03  
SSBOND  61 CYS G  416    CYS G  429                          1555   1555  2.03  
SSBOND  62 CYS G  423    CYS G  438                          1555   1555  2.03  
SSBOND  63 CYS G  440    CYS G  449                          1555   1555  2.03  
SSBOND  64 CYS G  456    CYS G  467                          1555   1555  2.03  
SSBOND  65 CYS G  461    CYS G  476                          1555   1555  2.03  
SSBOND  66 CYS G  478    CYS G  487                          1555   1555  2.03  
SSBOND  67 CYS G  494    CYS G  505                          1555   1555  2.03  
SSBOND  68 CYS G  499    CYS G  514                          1555   1555  2.03  
SSBOND  69 CYS G  516    CYS G  525                          1555   1555  2.03  
SSBOND  70 CYS H   50    CYS H   54                          1555   1555  2.03  
SSBOND  71 CYS H   61    CYS H   74                          1555   1555  2.03  
SSBOND  72 CYS H  175    CYS H  184                          1555   1555  2.03  
SSBOND  73 CYS H  188    CYS H  200                          1555   1555  2.03  
SSBOND  74 CYS H  208    CYS H  217                          1555   1555  2.03  
SSBOND  75 CYS H  222    CYS H  233                          1555   1555  2.03  
SSBOND  76 CYS H  226    CYS H  239                          1555   1555  2.03  
SSBOND  77 CYS H  241    CYS H  250                          1555   1555  2.03  
SSBOND  78 CYS H  253    CYS H  264                          1555   1555  2.04  
SSBOND  79 CYS H  259    CYS H  270                          1555   1555  2.03  
SSBOND  80 CYS H  272    CYS H  281                          1555   1555  2.03  
LINK         OD2 ASP A 414                CA    CA A 601     1555   1555  2.70  
LINK         OE1 GLU A 415                CA    CA A 601     1555   1555  2.65  
LINK         OD1 ASN A 431                CA    CA A 601     1555   1555  2.70  
LINK         O   THR A 432                CA    CA A 601     1555   1555  2.19  
LINK         O   LEU A 433                CA    CA A 601     1555   1555  3.14  
LINK         O   SER A 435                CA    CA A 601     1555   1555  2.51  
LINK         OG  SER A 435                 C1  BGC A 606     1555   1555  1.44  
LINK         OD1 ASP A 452                CA    CA A 602     1555   1555  2.41  
LINK         OD2 ASP A 452                CA    CA A 602     1555   1555  2.52  
LINK         O   VAL A 453                CA    CA A 602     1555   1555  2.51  
LINK         OE1 GLU A 455                CA    CA A 602     1555   1555  2.47  
LINK         OG  SER A 458                 C1  BGC A 604     1555   1555  1.43  
LINK         OG1 THR A 466                 C1  FUC A 605     1555   1555  1.43  
LINK         OD1 ASP A 469                CA    CA A 602     1555   1555  2.41  
LINK         OD2 ASP A 469                CA    CA A 602     1555   1555  2.40  
LINK         O   GLN A 470                CA    CA A 602     1555   1555  2.46  
LINK         OD1 ASN A 490                CA    CA A 603     1555   1555  2.44  
LINK         O   THR A 491                CA    CA A 603     1555   1555  2.42  
LINK         OE1 GLU A 493                CA    CA A 603     1555   1555  2.37  
LINK         OE2 GLU A 493                CA    CA A 603     1555   1555  2.40  
LINK         OG  SER A 496                 C1  BGC A 607     1555   1555  1.42  
LINK         OD1 ASP A 507                CA    CA A 603     1555   1555  2.39  
LINK         OD2 ASP A 507                CA    CA A 603     1555   1555  2.39  
LINK         O   LYS A 508                CA    CA A 603     1555   1555  2.65  
LINK         C   GLY B 152                 N   MLY B 153     1555   1555  1.33  
LINK         C   MLY B 153                 N   ASN B 154     1555   1555  1.33  
LINK         ND2 ASN B 161                 C1  NAG B 301     1555   1555  1.44  
LINK         C   CYS B 188                 N   MLY B 189     1555   1555  1.33  
LINK         C   MLY B 189                 N   MLY B 190     1555   1555  1.33  
LINK         C   MLY B 190                 N   ARG B 191     1555   1555  1.33  
LINK         C   GLY B 214                 N   MLY B 215     1555   1555  1.33  
LINK         C   MLY B 215                 N   TYR B 216     1555   1555  1.33  
LINK         C   SER B 234                 N   MLY B 235     1555   1555  1.33  
LINK         C   MLY B 235                 N   PRO B 236     1555   1555  1.34  
LINK         OD2 ASP C 414                CA    CA C 605     1555   1555  2.41  
LINK         OE1 GLU C 415                CA    CA C 605     1555   1555  2.42  
LINK         OD1 ASN C 431                CA    CA C 605     1555   1555  2.62  
LINK         O   THR C 432                CA    CA C 605     1555   1555  2.27  
LINK         O   SER C 435                CA    CA C 605     1555   1555  2.66  
LINK         OG  SER C 435                 C1  BGC C 603     1555   1555  1.44  
LINK         OD1 ASP C 452                CA    CA C 606     1555   1555  2.39  
LINK         OD2 ASP C 452                CA    CA C 606     1555   1555  2.47  
LINK         O   VAL C 453                CA    CA C 606     1555   1555  2.57  
LINK         OE1 GLU C 455                CA    CA C 606     1555   1555  2.47  
LINK         OG  SER C 458                 C1  BGC C 601     1555   1555  1.43  
LINK         OG1 THR C 466                 C1  FUC C 602     1555   1555  1.43  
LINK         OD1 ASP C 469                CA    CA C 606     1555   1555  2.41  
LINK         OD2 ASP C 469                CA    CA C 606     1555   1555  2.39  
LINK         O   GLN C 470                CA    CA C 606     1555   1555  2.45  
LINK         OD1 ASN C 490                CA    CA C 607     1555   1555  2.46  
LINK         O   THR C 491                CA    CA C 607     1555   1555  2.42  
LINK         OE1 GLU C 493                CA    CA C 607     1555   1555  2.36  
LINK         OE2 GLU C 493                CA    CA C 607     1555   1555  2.41  
LINK         OG  SER C 496                 C1  BGC C 604     1555   1555  1.43  
LINK         OD1 ASP C 507                CA    CA C 607     1555   1555  2.41  
LINK         OD2 ASP C 507                CA    CA C 607     1555   1555  2.41  
LINK         O   LYS C 508                CA    CA C 607     1555   1555  2.66  
LINK         C   GLY D 152                 N   MLY D 153     1555   1555  1.33  
LINK         C   MLY D 153                 N   ASN D 154     1555   1555  1.33  
LINK         ND2 ASN D 161                 C1  NAG D 301     1555   1555  1.44  
LINK         C   CYS D 188                 N   MLY D 189     1555   1555  1.33  
LINK         C   MLY D 189                 N   MLY D 190     1555   1555  1.33  
LINK         C   MLY D 190                 N   ARG D 191     1555   1555  1.33  
LINK         C   GLY D 214                 N   MLY D 215     1555   1555  1.33  
LINK         C   MLY D 215                 N   TYR D 216     1555   1555  1.33  
LINK         C   SER D 234                 N   MLY D 235     1555   1555  1.33  
LINK         C   MLY D 235                 N   PRO D 236     1555   1555  1.34  
LINK         OG  SER E 435                 C1  BGC E 905     1555   1555  1.44  
LINK         OD1 ASP E 452                CA    CA E 901     1555   1555  2.39  
LINK         OD2 ASP E 452                CA    CA E 901     1555   1555  2.46  
LINK         O   VAL E 453                CA    CA E 901     1555   1555  2.61  
LINK         OE1 GLU E 455                CA    CA E 901     1555   1555  2.45  
LINK         OG  SER E 458                 C1  BGC E 903     1555   1555  1.43  
LINK         OG1 THR E 466                 C1  FUC E 904     1555   1555  1.43  
LINK         OD1 ASP E 469                CA    CA E 901     1555   1555  2.39  
LINK         OD2 ASP E 469                CA    CA E 901     1555   1555  2.40  
LINK         O   GLN E 470                CA    CA E 901     1555   1555  2.45  
LINK         OD1 ASN E 490                CA    CA E 902     1555   1555  2.67  
LINK         O   THR E 491                CA    CA E 902     1555   1555  2.67  
LINK         OE1 GLU E 493                CA    CA E 902     1555   1555  2.36  
LINK         OE2 GLU E 493                CA    CA E 902     1555   1555  2.41  
LINK         OG  SER E 496                 C1  BGC E 906     1555   1555  1.43  
LINK         OD1 ASP E 507                CA    CA E 902     1555   1555  2.50  
LINK         OD2 ASP E 507                CA    CA E 902     1555   1555  2.47  
LINK         ND2 ASN F  78                 C1  NAG F 301     1555   1555  1.44  
LINK         C   GLY F 152                 N   MLY F 153     1555   1555  1.33  
LINK         C   MLY F 153                 N   ASN F 154     1555   1555  1.33  
LINK         ND2 ASN F 161                 C1  NAG F 302     1555   1555  1.44  
LINK         C   CYS F 188                 N   MLY F 189     1555   1555  1.33  
LINK         C   MLY F 189                 N   MLY F 190     1555   1555  1.33  
LINK         C   MLY F 190                 N   ARG F 191     1555   1555  1.33  
LINK         C   GLY F 214                 N   MLY F 215     1555   1555  1.33  
LINK         C   MLY F 215                 N   TYR F 216     1555   1555  1.33  
LINK         C   SER F 234                 N   MLY F 235     1555   1555  1.33  
LINK         C   MLY F 235                 N   PRO F 236     1555   1555  1.34  
LINK         OG  SER G 435                 C1  BGC G 905     1555   1555  1.44  
LINK         OD1 ASP G 452                CA    CA G 901     1555   1555  2.43  
LINK         OD2 ASP G 452                CA    CA G 901     1555   1555  2.45  
LINK         O   VAL G 453                CA    CA G 901     1555   1555  2.60  
LINK         OE1 GLU G 455                CA    CA G 901     1555   1555  2.46  
LINK         OG  SER G 458                 C1  BGC G 903     1555   1555  1.43  
LINK         OG1 THR G 466                 C1  FUC G 904     1555   1555  1.43  
LINK         OD1 ASP G 469                CA    CA G 901     1555   1555  2.38  
LINK         OD2 ASP G 469                CA    CA G 901     1555   1555  2.44  
LINK         O   GLN G 470                CA    CA G 901     1555   1555  2.46  
LINK         OD1 ASN G 490                CA    CA G 902     1555   1555  2.47  
LINK         O   THR G 491                CA    CA G 902     1555   1555  2.41  
LINK         OE1 GLU G 493                CA    CA G 902     1555   1555  2.35  
LINK         OE2 GLU G 493                CA    CA G 902     1555   1555  2.40  
LINK         OG  SER G 496                 C1  BGC G 906     1555   1555  1.42  
LINK         OD1 ASP G 507                CA    CA G 902     1555   1555  2.39  
LINK         OD2 ASP G 507                CA    CA G 902     1555   1555  2.41  
LINK         O   LYS G 508                CA    CA G 902     1555   1555  2.59  
LINK         ND2 ASN H  78                 C1  NAG H 301     1555   1555  1.44  
LINK         C   GLY H 152                 N   MLY H 153     1555   1555  1.33  
LINK         C   MLY H 153                 N   ASN H 154     1555   1555  1.33  
LINK         ND2 ASN H 161                 C1  NAG H 302     1555   1555  1.44  
LINK         C   CYS H 188                 N   MLY H 189     1555   1555  1.33  
LINK         C   MLY H 189                 N   MLY H 190     1555   1555  1.33  
LINK         C   MLY H 190                 N   ARG H 191     1555   1555  1.33  
LINK         C   GLY H 214                 N   MLY H 215     1555   1555  1.33  
LINK         C   MLY H 215                 N   TYR H 216     1555   1555  1.33  
LINK         C   SER H 234                 N   MLY H 235     1555   1555  1.33  
LINK         C   MLY H 235                 N   PRO H 236     1555   1555  1.35  
CISPEP   1 GLU B   51    PRO B   52          0        -0.63                     
CISPEP   2 ASN B  101    PRO B  102          0         2.07                     
CISPEP   3 GLU D   51    PRO D   52          0        -0.16                     
CISPEP   4 ASN D  101    PRO D  102          0         2.15                     
CISPEP   5 GLU F   51    PRO F   52          0        -0.30                     
CISPEP   6 ASN F  101    PRO F  102          0         1.84                     
CISPEP   7 GLU H   51    PRO H   52          0        -0.24                     
CISPEP   8 ASN H  101    PRO H  102          0         1.56                     
SITE     1 AC1  7 ASP A 414  GLU A 415  ASN A 431  THR A 432                    
SITE     2 AC1  7 LEU A 433  GLY A 434  SER A 435                               
SITE     1 AC2  5 ASP A 452  VAL A 453  GLU A 455  ASP A 469                    
SITE     2 AC2  5 GLN A 470                                                     
SITE     1 AC3  5 ASN A 490  THR A 491  GLU A 493  ASP A 507                    
SITE     2 AC3  5 LYS A 508                                                     
SITE     1 AC4  7 ASP C 414  GLU C 415  ASN C 431  THR C 432                    
SITE     2 AC4  7 LEU C 433  GLY C 434  SER C 435                               
SITE     1 AC5  5 ASP C 452  VAL C 453  GLU C 455  ASP C 469                    
SITE     2 AC5  5 GLN C 470                                                     
SITE     1 AC6  5 ASN C 490  THR C 491  GLU C 493  ASP C 507                    
SITE     2 AC6  5 LYS C 508                                                     
SITE     1 AC7  5 ASP E 452  VAL E 453  GLU E 455  ASP E 469                    
SITE     2 AC7  5 GLN E 470                                                     
SITE     1 AC8  6 ASN E 490  THR E 491  GLU E 493  ASP E 507                    
SITE     2 AC8  6 LYS E 508  ILE E 509                                          
SITE     1 AC9  5 ASP G 452  VAL G 453  GLU G 455  ASP G 469                    
SITE     2 AC9  5 GLN G 470                                                     
SITE     1 AD1  5 ASN G 490  THR G 491  GLU G 493  ASP G 507                    
SITE     2 AD1  5 LYS G 508                                                     
SITE     1 AD2  4 GLU A 415  SER A 435  PHE A 436  ASP B 218                    
SITE     1 AD3  3 GLU A 455  SER A 458  PHE A 474                               
SITE     1 AD4  6 THR A 466  MET A 479  HIS B  64  TYR B  65                    
SITE     2 AD4  6 GLN B  66  THR B 114                                          
SITE     1 AD5  3 GLU A 493  SER A 496  PHE A 512                               
SITE     1 AD6  4 ASN B 161  ASN F 161  ASN F 162  NAG F 302                    
SITE     1 AD7  4 GLU C 415  SER C 435  PHE C 436  ASP D 218                    
SITE     1 AD8  3 GLU C 455  SER C 458  PHE C 474                               
SITE     1 AD9  7 ASP C 464  THR C 466  MET C 479  HIS D  64                    
SITE     2 AD9  7 TYR D  65  GLN D  66  THR D 114                               
SITE     1 AE1  4 GLU C 493  SER C 496  PHE C 512  GLU G 483                    
SITE     1 AE2  4 GLU D 159  ASN D 161  ASN H 161  ASN H 162                    
SITE     1 AE3  5 GLU E 415  SER E 435  PHE E 436  ASP F 218                    
SITE     2 AE3  5 GLN F 219                                                     
SITE     1 AE4  3 GLU E 455  SER E 458  PHE E 474                               
SITE     1 AE5  5 ASP E 464  THR E 466  MET E 479  TYR F  65                    
SITE     2 AE5  5 THR F 114                                                     
SITE     1 AE6  4 GLU A 483  GLU E 493  SER E 496  PHE E 512                    
SITE     1 AE7  3 GLU A 511  CYS F  74  ASN F  78                               
SITE     1 AE8  4 ASN B 161  NAG B 301  ASN F 161  ARG F 166                    
SITE     1 AE9  4 GLU G 415  SER G 435  PHE G 436  ASP H 218                    
SITE     1 AF1  3 GLU G 455  SER G 458  PHE G 474                               
SITE     1 AF2  5 ASP G 464  THR G 466  MET G 479  TYR H  65                    
SITE     2 AF2  5 THR H 114                                                     
SITE     1 AF3  3 GLU G 493  SER G 496  PHE G 512                               
SITE     1 AF4  3 GLU C 511  CYS H  74  ASN H  78                               
SITE     1 AF5  5 ASN D 161  ASN D 162  GLU H 159  ASN H 161                    
SITE     2 AF5  5 ARG H 166                                                     
CRYST1   84.560   95.570  122.900  90.00  96.21  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011826  0.000000  0.001287        0.00000                         
SCALE2      0.000000  0.010464  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008185        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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