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Entry: 5L0S
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HEADER    TRANSFERASE                             28-JUL-16   5L0S              
TITLE     HUMAN POGLUT1 IN COMPLEX WITH FACTOR VII EGF1 AND UDP                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN O-GLUCOSYLTRANSFERASE 1;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CAP10-LIKE 46 KDA PROTEIN,HCLP46,KTEL MOTIF-CONTAINING      
COMPND   5 PROTEIN 1,MYELODYSPLASTIC SYNDROMES RELATIVE PROTEIN,O-              
COMPND   6 GLUCOSYLTRANSFERASE RUMI HOMOLOG,HRUMI,PROTEIN O-XYLOSYLTRANSFERASE; 
COMPND   7 EC: 2.4.1.-,2.4.2.26;                                                
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND  11 CHAIN: B;                                                            
COMPND  12 SYNONYM: PROCONVERTIN,SERUM PROTHROMBIN CONVERSION ACCELERATOR,SPCA; 
COMPND  13 EC: 3.4.21.21;                                                       
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: POGLUT1, C3ORF9, CLP46, KTELC1, MDSRP, MDS010, UNQ490/PRO1006; 
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HEK293S GNTI-;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PB-T-PAF;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: F7;                                                            
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PMAL                                      
KEYWDS    TRANSFERASE GLYCOSYLTRANSFERASE GT-B GLUCOSYLTRANSFERASE, TRANSFERASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.LI,J.M.RINI                                                         
REVDAT   2   30-AUG-17 5L0S    1       JRNL                                     
REVDAT   1   09-AUG-17 5L0S    0                                                
JRNL        AUTH   Z.LI,M.FISCHER,M.SATKUNARAJAH,D.ZHOU,S.G.WITHERS,J.M.RINI    
JRNL        TITL   STRUCTURAL BASIS OF NOTCH O-GLUCOSYLATION AND O-XYLOSYLATION 
JRNL        TITL 2 BY MAMMALIAN PROTEIN-O-GLUCOSYLTRANSFERASE 1 (POGLUT1).      
JRNL        REF    NAT COMMUN                    V.   8   185 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   28775322                                                     
JRNL        DOI    10.1038/S41467-017-00255-7                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 79612                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.140                           
REMARK   3   R VALUE            (WORKING SET) : 0.139                           
REMARK   3   FREE R VALUE                     : 0.159                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3981                            
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 44.0215 -  4.4016    0.98     2879   152  0.1657 0.1858        
REMARK   3     2  4.4016 -  3.4942    0.99     2764   145  0.1282 0.1470        
REMARK   3     3  3.4942 -  3.0526    1.00     2775   147  0.1320 0.1444        
REMARK   3     4  3.0526 -  2.7736    1.00     2744   144  0.1306 0.1387        
REMARK   3     5  2.7736 -  2.5748    1.00     2751   145  0.1273 0.1448        
REMARK   3     6  2.5748 -  2.4230    1.00     2725   143  0.1260 0.1463        
REMARK   3     7  2.4230 -  2.3017    1.00     2738   144  0.1211 0.1573        
REMARK   3     8  2.3017 -  2.2015    1.00     2727   144  0.1213 0.1713        
REMARK   3     9  2.2015 -  2.1167    1.00     2707   142  0.1181 0.1263        
REMARK   3    10  2.1167 -  2.0437    1.00     2732   144  0.1183 0.1432        
REMARK   3    11  2.0437 -  1.9798    1.00     2695   142  0.1172 0.1385        
REMARK   3    12  1.9798 -  1.9232    1.00     2714   143  0.1199 0.1394        
REMARK   3    13  1.9232 -  1.8726    1.00     2701   142  0.1220 0.1570        
REMARK   3    14  1.8726 -  1.8269    1.00     2711   143  0.1264 0.1504        
REMARK   3    15  1.8269 -  1.7853    1.00     2716   143  0.1327 0.1465        
REMARK   3    16  1.7853 -  1.7473    1.00     2681   141  0.1393 0.1602        
REMARK   3    17  1.7473 -  1.7124    1.00     2690   141  0.1427 0.1750        
REMARK   3    18  1.7124 -  1.6801    1.00     2696   142  0.1437 0.1477        
REMARK   3    19  1.6801 -  1.6501    1.00     2719   143  0.1519 0.1721        
REMARK   3    20  1.6501 -  1.6221    1.00     2674   141  0.1498 0.1719        
REMARK   3    21  1.6221 -  1.5959    1.00     2694   142  0.1586 0.1833        
REMARK   3    22  1.5959 -  1.5714    1.00     2659   140  0.1799 0.1848        
REMARK   3    23  1.5714 -  1.5483    1.00     2700   142  0.1846 0.1957        
REMARK   3    24  1.5483 -  1.5265    0.99     2664   140  0.1989 0.2448        
REMARK   3    25  1.5265 -  1.5058    1.00     2672   141  0.2122 0.2266        
REMARK   3    26  1.5058 -  1.4863    0.99     2679   141  0.2470 0.2333        
REMARK   3    27  1.4863 -  1.4677    0.96     2569   135  0.2604 0.2743        
REMARK   3    28  1.4677 -  1.4500    0.92     2455   129  0.2809 0.2743        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.870           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.87                          
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      :  0.008           3484                                  
REMARK   3   ANGLE     :  1.037           4741                                  
REMARK   3   CHIRALITY :  0.077            487                                  
REMARK   3   PLANARITY :  0.007            606                                  
REMARK   3   DIHEDRAL  : 16.238           1322                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 30 THROUGH 68 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2492  30.6788  34.7269              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1886 T22:   0.2903                                     
REMARK   3      T33:   0.1362 T12:  -0.0144                                     
REMARK   3      T13:   0.0200 T23:   0.0414                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0889 L22:   1.0140                                     
REMARK   3      L33:   1.8110 L12:  -0.7220                                     
REMARK   3      L13:   0.8707 L23:  -0.5216                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0797 S12:  -0.3268 S13:  -0.0096                       
REMARK   3      S21:   0.0819 S22:   0.1782 S23:   0.1347                       
REMARK   3      S31:  -0.0321 S32:  -0.4829 S33:  -0.1185                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 104 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1478  14.1425  30.9797              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2062 T22:   0.2201                                     
REMARK   3      T33:   0.3069 T12:   0.0813                                     
REMARK   3      T13:  -0.0638 T23:   0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1986 L22:   2.0660                                     
REMARK   3      L33:   3.9819 L12:  -0.7493                                     
REMARK   3      L13:   0.2786 L23:  -0.6038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0087 S12:  -0.0854 S13:  -0.3589                       
REMARK   3      S21:   0.0604 S22:  -0.0368 S23:  -0.1449                       
REMARK   3      S31:   0.4293 S32:   0.3246 S33:  -0.0474                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 105 THROUGH 139 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.8822  22.0327  27.9822              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1142 T22:   0.1565                                     
REMARK   3      T33:   0.1588 T12:   0.0249                                     
REMARK   3      T13:  -0.0245 T23:   0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4956 L22:   2.1973                                     
REMARK   3      L33:   2.8180 L12:   0.1530                                     
REMARK   3      L13:   1.0860 L23:  -0.0051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0425 S12:  -0.0756 S13:  -0.1305                       
REMARK   3      S21:   0.0528 S22:  -0.0018 S23:  -0.1816                       
REMARK   3      S31:   0.0326 S32:   0.2421 S33:  -0.0190                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 197 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7152  27.4775  21.3237              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1102 T22:   0.1116                                     
REMARK   3      T33:   0.1243 T12:  -0.0046                                     
REMARK   3      T13:  -0.0088 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3764 L22:   1.6933                                     
REMARK   3      L33:   1.5576 L12:  -0.4338                                     
REMARK   3      L13:   0.4165 L23:  -0.5711                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0518 S12:   0.0356 S13:  -0.0403                       
REMARK   3      S21:  -0.0047 S22:   0.0066 S23:  -0.0565                       
REMARK   3      S31:  -0.0131 S32:   0.1154 S33:  -0.0293                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 227 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2093  31.8378   8.6209              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1425 T22:   0.1839                                     
REMARK   3      T33:   0.1315 T12:   0.0004                                     
REMARK   3      T13:  -0.0094 T23:   0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3868 L22:   2.3400                                     
REMARK   3      L33:   2.3828 L12:  -0.4198                                     
REMARK   3      L13:   0.4930 L23:   0.3066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1195 S12:   0.1968 S13:  -0.0611                       
REMARK   3      S21:  -0.1537 S22:  -0.0257 S23:   0.1844                       
REMARK   3      S31:  -0.0187 S32:  -0.1760 S33:  -0.0950                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 228 THROUGH 248 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.6140  24.4993   2.0898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2293 T22:   0.2333                                     
REMARK   3      T33:   0.1625 T12:   0.0141                                     
REMARK   3      T13:  -0.0499 T23:  -0.0345                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6060 L22:   1.0390                                     
REMARK   3      L33:   3.0143 L12:   1.4862                                     
REMARK   3      L13:  -0.2465 L23:   0.6117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1969 S12:   0.7825 S13:  -0.4751                       
REMARK   3      S21:  -0.3282 S22:  -0.1359 S23:   0.0847                       
REMARK   3      S31:   0.2186 S32:   0.0461 S33:  -0.0674                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 249 THROUGH 279 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.3910  31.5169   9.9377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1357 T22:   0.1451                                     
REMARK   3      T33:   0.1058 T12:  -0.0003                                     
REMARK   3      T13:  -0.0122 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6142 L22:   1.6156                                     
REMARK   3      L33:   1.8165 L12:  -0.0610                                     
REMARK   3      L13:   0.1687 L23:  -0.0105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0558 S12:   0.1746 S13:  -0.0325                       
REMARK   3      S21:  -0.1750 S22:   0.0459 S23:   0.0922                       
REMARK   3      S31:  -0.0376 S32:  -0.0273 S33:  -0.0900                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 280 THROUGH 331 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9127  30.5712  21.1033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1208 T22:   0.1594                                     
REMARK   3      T33:   0.1405 T12:   0.0011                                     
REMARK   3      T13:  -0.0006 T23:   0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1683 L22:   1.0583                                     
REMARK   3      L33:   1.5762 L12:  -0.3501                                     
REMARK   3      L13:   0.3427 L23:  -0.5797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0144 S12:  -0.0450 S13:  -0.1053                       
REMARK   3      S21:   0.0289 S22:   0.1158 S23:   0.1417                       
REMARK   3      S31:  -0.0189 S32:  -0.2589 S33:  -0.1221                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 349 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8149  42.0445  25.7739              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2638 T22:   0.1579                                     
REMARK   3      T33:   0.1966 T12:   0.0550                                     
REMARK   3      T13:   0.0237 T23:   0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2715 L22:   1.1922                                     
REMARK   3      L33:   3.7791 L12:  -0.6888                                     
REMARK   3      L13:   3.7366 L23:  -0.5393                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2391 S12:  -0.2356 S13:   0.5761                       
REMARK   3      S21:   0.2326 S22:   0.1367 S23:   0.1234                       
REMARK   3      S31:  -0.5022 S32:  -0.2943 S33:   0.1313                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 350 THROUGH 385 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0960  23.9078  34.6518              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1676 T22:   0.2248                                     
REMARK   3      T33:   0.2092 T12:   0.0132                                     
REMARK   3      T13:  -0.0619 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4021 L22:   1.9414                                     
REMARK   3      L33:   1.8238 L12:  -0.5407                                     
REMARK   3      L13:   0.2108 L23:  -0.2414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0393 S12:  -0.2350 S13:  -0.0765                       
REMARK   3      S21:   0.2643 S22:   0.0323 S23:  -0.4091                       
REMARK   3      S31:   0.0736 S32:   0.3734 S33:  -0.0190                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 47 THROUGH 71 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  26.1632  18.1502   7.2699              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3213 T22:   0.2602                                     
REMARK   3      T33:   0.2955 T12:   0.0474                                     
REMARK   3      T13:   0.0126 T23:  -0.0600                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6822 L22:   4.2242                                     
REMARK   3      L33:   5.9624 L12:  -2.3767                                     
REMARK   3      L13:  -1.0800 L23:  -0.1951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0491 S12:   0.1780 S13:  -0.6650                       
REMARK   3      S21:  -0.1245 S22:  -0.1435 S23:  -0.0915                       
REMARK   3      S31:   0.7727 S32:   0.1932 S33:   0.1376                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 72 THROUGH 85 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  35.7351  26.6231   4.5462              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3477 T22:   0.4520                                     
REMARK   3      T33:   0.5486 T12:   0.0152                                     
REMARK   3      T13:   0.1414 T23:  -0.0710                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6494 L22:   2.5072                                     
REMARK   3      L33:   6.4586 L12:   2.4488                                     
REMARK   3      L13:   0.5059 L23:   0.9138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2056 S12:   0.3222 S13:   0.2486                       
REMARK   3      S21:  -0.5250 S22:   0.2964 S23:  -1.2609                       
REMARK   3      S31:  -0.1228 S32:   1.2457 S33:  -0.1939                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5L0S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223029.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79619                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.6100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.89800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.680                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG5000 MME, 50 MM MES PH 6.5, 2MM   
REMARK 280  CACL2, 250MM NACL, 5% GLYCEROL, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       35.29000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.27500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.46000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.27500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.29000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.46000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 3270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 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     GLY A    29                                                      
REMARK 465     GLY B    44                                                      
REMARK 465     SER B    45                                                      
REMARK 465     ASP B    46                                                      
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     SER A  30    N    CA   CB   OG                                   
REMARK 470     LYS A 378    CG   CD   CE   NZ                                   
REMARK 470     LEU B  65    CG   CD1  CD2                                       
REMARK 470     GLN B  66    CG   CD   OE1  NE2                                  
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   O    HOH A  1119     O    HOH A  1133              2.02            
REMARK 500   O    HOH A  1210     O    HOH A  1394              2.02            
REMARK 500   O    HOH A  1300     O    HOH A  1359              2.04            
REMARK 500   O    HOH A  1296     O    HOH A  1346              2.04            
REMARK 500   O    HOH A  1232     O    HOH A  1339              2.10            
REMARK 500   O    HOH A  1346     O    HOH A  1347              2.10            
REMARK 500   O    HOH B   217     O    HOH B   229              2.12            
REMARK 500   O    HOH A  1206     O    HOH A  1425              2.12            
REMARK 500   O    HOH B   221     O    HOH B   230              2.17            
REMARK 500   O    HOH A  1323     O    HOH A  1390              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1345     O    HOH A  1363     4456     2.06            
REMARK 500   O    HOH A  1172     O    HOH A  1264     2564     2.14            
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    ALA A 275     -142.11   -127.30                                   
REMARK 500    ASP A 295       22.97   -143.85                                   
REMARK 500    TRP A 308      -25.57     73.15                                   
REMARK 500    SER B  53       64.60     61.22                                   
REMARK 500    SER B  67     -156.67   -125.92                                   
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 B 101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B  47   O                                                      
REMARK 620 2 ASP B  63   OD1  91.1                                              
REMARK 620 3 ASP B  63   OD2  74.5  44.3                                        
REMARK 620 4 SER B  67   O   146.5  64.8  99.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UDP A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1001        
REMARK 800  bound to ASN A 40                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1002        
REMARK 800  bound to ASN A 53                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1003        
REMARK 800  bound to ASN A 204                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5L0R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5L0T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5L0U   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5L0V   RELATED DB: PDB                                   
DBREF  5L0S A   29   385  UNP    Q8NBL1   PGLT1_HUMAN     29    385             
DBREF  5L0S B   45    85  UNP    P08709   FA7_HUMAN      105    145             
SEQADV 5L0S GLY B   44  UNP  P08709              EXPRESSION TAG                 
SEQRES   1 A  357  GLY SER LYS TRP LYS VAL PHE ILE ASP GLN ILE ASN ARG          
SEQRES   2 A  357  SER LEU GLU ASN TYR GLU PRO CYS SER SER GLN ASN CYS          
SEQRES   3 A  357  SER CYS TYR HIS GLY VAL ILE GLU GLU ASP LEU THR PRO          
SEQRES   4 A  357  PHE ARG GLY GLY ILE SER ARG LYS MET MET ALA GLU VAL          
SEQRES   5 A  357  VAL ARG ARG LYS LEU GLY THR HIS TYR GLN ILE THR LYS          
SEQRES   6 A  357  ASN ARG LEU TYR ARG GLU ASN ASP CYS MET PHE PRO SER          
SEQRES   7 A  357  ARG CYS SER GLY VAL GLU HIS PHE ILE LEU GLU VAL ILE          
SEQRES   8 A  357  GLY ARG LEU PRO ASP MET GLU MET VAL ILE ASN VAL ARG          
SEQRES   9 A  357  ASP TYR PRO GLN VAL PRO LYS TRP MET GLU PRO ALA ILE          
SEQRES  10 A  357  PRO VAL PHE SER PHE SER LYS THR SER GLU TYR HIS ASP          
SEQRES  11 A  357  ILE MET TYR PRO ALA TRP THR PHE TRP GLU GLY GLY PRO          
SEQRES  12 A  357  ALA VAL TRP PRO ILE TYR PRO THR GLY LEU GLY ARG TRP          
SEQRES  13 A  357  ASP LEU PHE ARG GLU ASP LEU VAL ARG SER ALA ALA GLN          
SEQRES  14 A  357  TRP PRO TRP LYS LYS LYS ASN SER THR ALA TYR PHE ARG          
SEQRES  15 A  357  GLY SER ARG THR SER PRO GLU ARG ASP PRO LEU ILE LEU          
SEQRES  16 A  357  LEU SER ARG LYS ASN PRO LYS LEU VAL ASP ALA GLU TYR          
SEQRES  17 A  357  THR LYS ASN GLN ALA TRP LYS SER MET LYS ASP THR LEU          
SEQRES  18 A  357  GLY LYS PRO ALA ALA LYS ASP VAL HIS LEU VAL ASP HIS          
SEQRES  19 A  357  CYS LYS TYR LYS TYR LEU PHE ASN PHE ARG GLY VAL ALA          
SEQRES  20 A  357  ALA SER PHE ARG PHE LYS HIS LEU PHE LEU CYS GLY SER          
SEQRES  21 A  357  LEU VAL PHE HIS VAL GLY ASP GLU TRP LEU GLU PHE PHE          
SEQRES  22 A  357  TYR PRO GLN LEU LYS PRO TRP VAL HIS TYR ILE PRO VAL          
SEQRES  23 A  357  LYS THR ASP LEU SER ASN VAL GLN GLU LEU LEU GLN PHE          
SEQRES  24 A  357  VAL LYS ALA ASN ASP ASP VAL ALA GLN GLU ILE ALA GLU          
SEQRES  25 A  357  ARG GLY SER GLN PHE ILE ARG ASN HIS LEU GLN MET ASP          
SEQRES  26 A  357  ASP ILE THR CYS TYR TRP GLU ASN LEU LEU SER GLU TYR          
SEQRES  27 A  357  SER LYS PHE LEU SER TYR ASN VAL THR ARG ARG LYS GLY          
SEQRES  28 A  357  TYR ASP GLN ILE ILE PRO                                      
SEQRES   1 B   42  GLY SER ASP GLY ASP GLN CYS ALA SER SER PRO CYS GLN          
SEQRES   2 B   42  ASN GLY GLY SER CYS LYS ASP GLN LEU GLN SER TYR ILE          
SEQRES   3 B   42  CYS PHE CYS LEU PRO ALA PHE GLU GLY ARG ASN CYS GLU          
SEQRES   4 B   42  THR HIS LYS                                                  
HET    NAG  A1001      14                                                       
HET    NAG  A1002      28                                                       
HET    NAG  A1003      28                                                       
HET    UDP  A1004      36                                                       
HET     CL  A1005       1                                                       
HET    GOL  A1006      14                                                       
HET    GOL  A1007      14                                                       
HET     CA  B 101       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     UDP URIDINE-5'-DIPHOSPHATE                                           
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   6  UDP    C9 H14 N2 O12 P2                                             
FORMUL   7   CL    CL 1-                                                        
FORMUL   8  GOL    2(C3 H8 O3)                                                  
FORMUL  10   CA    CA 2+                                                        
FORMUL  11  HOH   *377(H2 O)                                                    
HELIX    1 AA1 TRP A   32  TYR A   46  1                                  15    
HELIX    2 AA2 ASN A   53  CYS A   56  5                                   4    
HELIX    3 AA3 TYR A   57  THR A   66  1                                  10    
HELIX    4 AA4 PRO A   67  ARG A   69  5                                   3    
HELIX    5 AA5 SER A   73  ARG A   83  1                                  11    
HELIX    6 AA6 PHE A  104  ILE A  119  1                                  16    
HELIX    7 AA7 GLY A  120  LEU A  122  5                                   3    
HELIX    8 AA8 ALA A  163  TRP A  167  5                                   5    
HELIX    9 AA9 ARG A  183  TRP A  198  1                                  16    
HELIX   10 AB1 PRO A  199  LYS A  203  5                                   5    
HELIX   11 AB2 SER A  215  GLU A  217  5                                   3    
HELIX   12 AB3 ARG A  218  ASN A  228  1                                  11    
HELIX   13 AB4 SER A  244  LEU A  249  5                                   6    
HELIX   14 AB5 HIS A  258  CYS A  263  5                                   6    
HELIX   15 AB6 PHE A  278  CYS A  286  1                                   9    
HELIX   16 AB7 PHE A  301  LEU A  305  5                                   5    
HELIX   17 AB8 ASN A  320  ASN A  331  1                                  12    
HELIX   18 AB9 ASN A  331  LEU A  350  1                                  20    
HELIX   19 AC1 GLN A  351  LYS A  368  1                                  18    
HELIX   20 AC2 ASP B   48  SER B   53  5                                   6    
SHEET    1 AA1 4 MET A 125  ILE A 129  0                                        
SHEET    2 AA1 4 THR A  87  THR A  92 -1  N  ILE A  91   O  MET A 125           
SHEET    3 AA1 4 ARG A  95  ARG A  98 -1  O  TYR A  97   N  GLN A  90           
SHEET    4 AA1 4 ASP A 381  ILE A 383 -1  O  ILE A 383   N  LEU A  96           
SHEET    1 AA2 2 PHE A 148  SER A 149  0                                        
SHEET    2 AA2 2 ILE A 159  MET A 160  1  O  ILE A 159   N  SER A 149           
SHEET    1 AA3 2 ALA A 207  GLY A 211  0                                        
SHEET    2 AA3 2 VAL A 232  TYR A 236  1  O  ASP A 233   N  ALA A 207           
SHEET    1 AA4 3 TYR A 267  ASN A 270  0                                        
SHEET    2 AA4 3 LEU A 289  VAL A 293  1  O  VAL A 293   N  ASN A 270           
SHEET    3 AA4 3 ILE A 312  VAL A 314  1  O  ILE A 312   N  VAL A 290           
SHEET    1 AA5 2 SER B  60  GLN B  64  0                                        
SHEET    2 AA5 2 SER B  67  PHE B  71 -1  O  PHE B  71   N  SER B  60           
SHEET    1 AA6 2 PHE B  76  GLU B  77  0                                        
SHEET    2 AA6 2 THR B  83  HIS B  84 -1  O  THR B  83   N  GLU B  77           
SSBOND   1 CYS A   49    CYS A   56                          1555   1555  2.01  
SSBOND   2 CYS A   54    CYS A  357                          1555   1555  2.09  
SSBOND   3 CYS A  102    CYS A  108                          1555   1555  2.04  
SSBOND   4 CYS A  263    CYS A  286                          1555   1555  2.09  
SSBOND   5 CYS B   50    CYS B   61                          1555   1555  2.03  
SSBOND   6 CYS B   55    CYS B   70                          1555   1555  2.03  
SSBOND   7 CYS B   72    CYS B   81                          1555   1555  2.08  
LINK         ND2 ASN A  40                 C1  NAG A1001     1555   1555  1.43  
LINK         ND2 ASN A  53                 C1  NAG A1002     1555   1555  1.44  
LINK         ND2 ASN A 204                 C1  NAG A1003     1555   1555  1.42  
LINK         O   GLY B  47                CA    CA B 101     1555   1555  2.72  
LINK         OD1 ASP B  63                CA    CA B 101     1555   1555  2.38  
LINK         OD2 ASP B  63                CA    CA B 101     1555   1555  3.15  
LINK         O   SER B  67                CA    CA B 101     1555   1555  3.14  
CISPEP   1 GLU A  142    PRO A  143          0        -0.27                     
CISPEP   2 TRP A  174    PRO A  175          0         2.82                     
CISPEP   3 ILE A  384    PRO A  385          0         3.29                     
SITE     1 AC1 21 VAL A 173  ILE A 176  TYR A 177  LEU A 181                    
SITE     2 AC1 21 ARG A 210  GLY A 211  SER A 212  THR A 214                    
SITE     3 AC1 21 ARG A 218  THR A 237  ASP A 256  VAL A 257                    
SITE     4 AC1 21 LEU A 259  GLY A 273  SER A 277  ARG A 279                    
SITE     5 AC1 21 GOL A1006  HOH A1132  HOH A1179  HOH A1271                    
SITE     6 AC1 21 HOH B 223                                                     
SITE     1 AC2  3 PHE A 104  PRO A 105  SER A 106                               
SITE     1 AC3  9 ARG A 107  ASP A 133  PRO A 171  ALA A 276                    
SITE     2 AC3  9 SER A 277  PHE A 278  UDP A1004  HOH A1219                    
SITE     3 AC3  9 SER B  52                                                     
SITE     1 AC4 10 ARG A 213  ASN A 239  ALA A 241  TRP A 242                    
SITE     2 AC4 10 ASP A 247  HOH A1144  HOH A1241  HOH A1268                    
SITE     3 AC4 10 HOH A1318  ALA B  51                                          
SITE     1 AC5  5 GLY B  47  GLN B  49  ASP B  63  GLN B  66                    
SITE     2 AC5  5 SER B  67                                                     
SITE     1 AC6  2 ASN A  40  GLU A  44                                          
SITE     1 AC7 14 SER A  51  ASN A  53  SER A  55  ILE A 176                    
SITE     2 AC7 14 VAL A 257  HIS A 258  ASP A 261  HOH A1115                    
SITE     3 AC7 14 HOH A1203  HOH A1204  HOH A1264  HOH A1284                    
SITE     4 AC7 14 HOH A1297  HOH A1329                                          
SITE     1 AC8 12 GLY A 120  ARG A 121  ASN A 204  THR A 206                    
SITE     2 AC8 12 ASP A 233  TYR A 265  HOH A1142  HOH A1157                    
SITE     3 AC8 12 HOH A1190  HOH A1243  HOH A1260  HOH A1334                    
CRYST1   70.580   76.920   82.550  90.00  90.00  90.00 P 21 21 21    4          
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      0.014168  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013001  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012114        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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