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Database: PDB
Entry: 5UB5
LinkDB: 5UB5
Original site: 5UB5 
HEADER    TRANSFERASE                             20-DEC-16   5UB5              
TITLE     HUMAN POGLUT1 IN COMPLEX WITH HUMAN NOTCH1 EGF12 S458T MUTANT AND UDP 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN O-GLUCOSYLTRANSFERASE 1;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 29-385;                                       
COMPND   5 SYNONYM: CAP10-LIKE 46 KDA PROTEIN,HCLP46,KTEL MOTIF-CONTAINING      
COMPND   6 PROTEIN 1,MYELODYSPLASTIC SYNDROMES RELATIVE PROTEIN,O-              
COMPND   7 GLUCOSYLTRANSFERASE RUMI HOMOLOG,HRUMI,PROTEIN O-XYLOSYLTRANSFERASE; 
COMPND   8 EC: 2.4.1.-,2.4.2.26;                                                
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: UNP RESIDUES 452-491;                                      
COMPND  14 SYNONYM: HN1,TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1;           
COMPND  15 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_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;                          
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PB-T-PAF;                                 
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: NOTCH1, TAN1;                                                  
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)                                 
KEYWDS    TRANSFERASE, GLYCOSYLTRANSFERASE, GT-B GLUCOSYLTRANSFERASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.LI,J.M.RINI                                                         
REVDAT   3   04-APR-18 5UB5    1       SOURCE REMARK                            
REVDAT   2   30-AUG-17 5UB5    1       JRNL                                     
REVDAT   1   09-AUG-17 5UB5    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.    2.09 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 26479                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.160                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1365                            
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 20.8968 -  4.4866    0.99     2687   130  0.1461 0.1672        
REMARK   3     2  4.4866 -  3.5669    1.00     2565   145  0.1269 0.1644        
REMARK   3     3  3.5669 -  3.1177    1.00     2548   139  0.1413 0.1877        
REMARK   3     4  3.1177 -  2.8334    1.00     2538   132  0.1587 0.1901        
REMARK   3     5  2.8334 -  2.6307    1.00     2508   143  0.1504 0.2000        
REMARK   3     6  2.6307 -  2.4759    1.00     2510   152  0.1553 0.2229        
REMARK   3     7  2.4759 -  2.3521    1.00     2514   136  0.1544 0.1953        
REMARK   3     8  2.3521 -  2.2498    1.00     2482   139  0.1641 0.2129        
REMARK   3     9  2.2498 -  2.1633    1.00     2504   133  0.1934 0.2484        
REMARK   3    10  2.1633 -  2.0887    0.90     2258   116  0.2369 0.2787        
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.44                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.95                          
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           3483                                  
REMARK   3   ANGLE     :  1.235           4752                                  
REMARK   3   CHIRALITY :  0.071            496                                  
REMARK   3   PLANARITY :  0.010            609                                  
REMARK   3   DIHEDRAL  : 12.287           2072                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 30 THROUGH 68 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0961  30.3977  34.9009              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1910 T22:   0.4234                                     
REMARK   3      T33:   0.1209 T12:  -0.0253                                     
REMARK   3      T13:   0.0603 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9881 L22:   0.7756                                     
REMARK   3      L33:   0.0547 L12:  -0.4957                                     
REMARK   3      L13:   0.0379 L23:   0.0494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1598 S12:  -0.1857 S13:   0.0435                       
REMARK   3      S21:   0.2514 S22:   0.0659 S23:   0.0150                       
REMARK   3      S31:   0.2015 S32:  -0.5032 S33:  -0.2184                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 104 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  32.2411  12.9245  31.9428              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3353 T22:   0.3933                                     
REMARK   3      T33:   0.2832 T12:   0.2080                                     
REMARK   3      T13:  -0.0159 T23:   0.0638                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1880 L22:   0.0197                                     
REMARK   3      L33:   0.2499 L12:  -0.0092                                     
REMARK   3      L13:  -0.2068 L23:  -0.0100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0749 S12:  -0.3330 S13:  -0.2480                       
REMARK   3      S21:   0.0912 S22:   0.0338 S23:  -0.1472                       
REMARK   3      S31:   0.3284 S32:   0.3695 S33:   0.0028                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 105 THROUGH 139 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.8541  20.8123  28.9275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2353 T22:   0.2171                                     
REMARK   3      T33:   0.1867 T12:   0.0637                                     
REMARK   3      T13:  -0.0209 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1284 L22:   0.7454                                     
REMARK   3      L33:   0.5596 L12:  -0.0240                                     
REMARK   3      L13:  -0.0093 L23:   0.2975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0572 S12:  -0.1373 S13:  -0.1560                       
REMARK   3      S21:   0.1224 S22:   0.1213 S23:  -0.1970                       
REMARK   3      S31:   0.3198 S32:   0.3852 S33:   0.0385                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 197 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8340  26.1078  21.8291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1469 T22:   0.0761                                     
REMARK   3      T33:   0.1487 T12:   0.0198                                     
REMARK   3      T13:   0.0105 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6668 L22:   0.4038                                     
REMARK   3      L33:   0.5222 L12:  -0.3536                                     
REMARK   3      L13:   0.0831 L23:   0.3075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0207 S12:  -0.0441 S13:  -0.0059                       
REMARK   3      S21:   0.0426 S22:   0.0334 S23:  -0.0214                       
REMARK   3      S31:   0.0779 S32:   0.1076 S33:   0.1906                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 198 THROUGH 248 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5477  27.1114   6.2448              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1207 T22:   0.1948                                     
REMARK   3      T33:   0.1305 T12:  -0.0063                                     
REMARK   3      T13:  -0.0093 T23:  -0.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7106 L22:   0.1103                                     
REMARK   3      L33:   0.8080 L12:   0.0271                                     
REMARK   3      L13:  -0.1584 L23:   0.0756                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0550 S12:   0.3539 S13:  -0.0685                       
REMARK   3      S21:  -0.0284 S22:  -0.0338 S23:   0.0416                       
REMARK   3      S31:   0.0996 S32:  -0.3462 S33:   0.0817                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 249 THROUGH 349 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8781  31.5323  18.8246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0922 T22:   0.1281                                     
REMARK   3      T33:   0.1069 T12:  -0.0105                                     
REMARK   3      T13:   0.0038 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7324 L22:   0.3367                                     
REMARK   3      L33:   0.8549 L12:  -0.1490                                     
REMARK   3      L13:  -0.1960 L23:  -0.0691                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0151 S12:   0.0087 S13:   0.0713                       
REMARK   3      S21:   0.0128 S22:   0.0007 S23:   0.0673                       
REMARK   3      S31:   0.0168 S32:  -0.3123 S33:   0.0063                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 350 THROUGH 385 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0849  22.9031  35.4433              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2195 T22:   0.3379                                     
REMARK   3      T33:   0.1767 T12:   0.1379                                     
REMARK   3      T13:  -0.0144 T23:   0.0159                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5383 L22:   0.3539                                     
REMARK   3      L33:   0.8362 L12:  -0.3537                                     
REMARK   3      L13:   0.2733 L23:  -0.3474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1570 S12:  -0.4443 S13:   0.0781                       
REMARK   3      S21:   0.1491 S22:   0.1780 S23:  -0.3203                       
REMARK   3      S31:   0.1153 S32:   0.4894 S33:   0.1390                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 452 THROUGH 477 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.2218  15.5507   8.1296              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3471 T22:   0.1542                                     
REMARK   3      T33:   0.2688 T12:   0.0832                                     
REMARK   3      T13:   0.0457 T23:  -0.0878                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2486 L22:   0.0822                                     
REMARK   3      L33:   0.1809 L12:  -0.1441                                     
REMARK   3      L13:   0.2073 L23:  -0.1157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0098 S12:   0.1402 S13:  -0.2956                       
REMARK   3      S21:  -0.0033 S22:  -0.0806 S23:   0.0434                       
REMARK   3      S31:   0.4342 S32:   0.1862 S33:  -0.0860                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 478 THROUGH 491 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2665  24.4929   5.5307              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3110 T22:   0.3550                                     
REMARK   3      T33:   0.3030 T12:  -0.0486                                     
REMARK   3      T13:   0.0905 T23:  -0.0821                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1014 L22:   0.0559                                     
REMARK   3      L33:   0.1684 L12:  -0.0737                                     
REMARK   3      L13:   0.1289 L23:  -0.0956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1719 S12:   0.1514 S13:   0.0471                       
REMARK   3      S21:  -0.1454 S22:   0.3893 S23:  -0.2828                       
REMARK   3      S31:   0.0496 S32:   0.1043 S33:   0.0328                       
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 5UB5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000225544.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER TURBO X-RAY SOURCE          
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : BRUKER PHOTON 100                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SAINT                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26486                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.089                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 11.00                              
REMARK 200  R MERGE                    (I) : 0.09068                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.7400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54860                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.160                              
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: 5L0R                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (V/V) PEG5000 MME, 50 MM MES PH      
REMARK 280  6.5, 2MM CACL2, 250MM NACL, 5% (V/V) 2-METHYL-2,4-PENTANEDIOL,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, 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       35.47550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.79150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.03600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.79150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.47550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.03600            
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: 2870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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   450                                                      
REMARK 465     SER B   451                                                      
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 243    CG   CD   CE   NZ                                   
REMARK 470     GLU A 323    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 378    CG   CD   CE   NZ                                   
REMARK 470     ILE B 471    CG1  CG2  CD1                                       
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   617     O    HOH A   760              2.09            
REMARK 500   O    HOH A   755     O    HOH A   783              2.16            
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    ARG A 183       69.08     39.12                                   
REMARK 500    ALA A 275     -141.58   -128.89                                   
REMARK 500    ASP A 295       26.07   -142.51                                   
REMARK 500    TRP A 308      -20.17     73.44                                   
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 B1001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 452   OD1                                                    
REMARK 620 2 ASP B 452   OD2  43.1                                              
REMARK 620 3 VAL B 453   O    90.6  75.8                                        
REMARK 620 4 GLU B 455   OE1 135.9 145.8  69.9                                  
REMARK 620 5 ASP B 469   OD1 122.5  83.1  94.3  98.9                            
REMARK 620 6 GLN B 470   O    68.8  78.1 153.9 136.1  84.2                      
REMARK 620 7 GLU B 473   O   118.9 142.5 141.6  71.7  89.8  64.5                
REMARK 620 8 HOH B1103   O    66.0 105.3  86.4  73.4 171.5  98.9  84.5          
REMARK 620 N                    1     2     3     4     5     6     7           
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 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 401 bound   
REMARK 800  to ASN A 53                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 402 bound   
REMARK 800  to ASN A 204                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 403 bound   
REMARK 800  to ASN A 373                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5L0R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5L0S   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  5UB5 A   29   385  UNP    Q8NBL1   PGLT1_HUMAN     29    385             
DBREF  5UB5 B  452   491  UNP    P46531   NOTC1_HUMAN    452    491             
SEQADV 5UB5 GLY B  450  UNP  P46531              EXPRESSION TAG                 
SEQADV 5UB5 SER B  451  UNP  P46531              EXPRESSION TAG                 
SEQADV 5UB5 THR B  458  UNP  P46531    SER   458 ENGINEERED MUTATION            
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 VAL ASN GLU CYS VAL THR ASN PRO CYS GLN          
SEQRES   2 B   42  ASN ASP ALA THR CYS LEU ASP GLN ILE GLY GLU PHE GLN          
SEQRES   3 B   42  CYS ILE CYS MET PRO GLY TYR GLU GLY VAL HIS CYS GLU          
SEQRES   4 B   42  VAL ASN THR                                                  
HET    NAG  A 401      28                                                       
HET    NAG  A 402      28                                                       
HET    NAG  A 403      28                                                       
HET    UDP  A 404      36                                                       
HET     CA  B1001       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     UDP URIDINE-5'-DIPHOSPHATE                                           
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   6  UDP    C9 H14 N2 O12 P2                                             
FORMUL   7   CA    CA 2+                                                        
FORMUL   8  HOH   *337(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 ASN B  454  ASN B  459  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 THR B 466  GLN B 470  0                                        
SHEET    2 AA5 2 GLU B 473  ILE B 477 -1  O  GLN B 475   N  LEU B 468           
SHEET    1 AA6 2 TYR B 482  GLU B 483  0                                        
SHEET    2 AA6 2 VAL B 489  ASN B 490 -1  O  VAL B 489   N  GLU B 483           
SSBOND   1 CYS A   49    CYS A   56                          1555   1555  2.02  
SSBOND   2 CYS A   54    CYS A  357                          1555   1555  2.15  
SSBOND   3 CYS A  102    CYS A  108                          1555   1555  2.09  
SSBOND   4 CYS A  263    CYS A  286                          1555   1555  2.18  
SSBOND   5 CYS B  456    CYS B  467                          1555   1555  2.11  
SSBOND   6 CYS B  461    CYS B  476                          1555   1555  2.05  
SSBOND   7 CYS B  478    CYS B  487                          1555   1555  2.07  
LINK         ND2 ASN A  53                 C1  NAG A 401     1555   1555  1.44  
LINK         ND2 ASN A 204                 C1  NAG A 402     1555   1555  1.43  
LINK         ND2 ASN A 373                 C1  NAG A 403     1555   1555  1.43  
LINK         OD1 ASP B 452                CA    CA B1001     1555   1555  3.19  
LINK         OD2 ASP B 452                CA    CA B1001     1555   1555  2.61  
LINK         O   VAL B 453                CA    CA B1001     1555   1555  2.52  
LINK         OE1 GLU B 455                CA    CA B1001     1555   1555  2.47  
LINK         OD1 ASP B 469                CA    CA B1001     1555   1555  2.28  
LINK         O   GLN B 470                CA    CA B1001     1555   1555  2.52  
LINK         O   GLU B 473                CA    CA B1001     1555   1555  2.87  
LINK        CA    CA B1001                 O   HOH B1103     1555   1555  2.15  
CISPEP   1 GLU A  142    PRO A  143          0        -6.25                     
CISPEP   2 TRP A  174    PRO A  175          0         2.39                     
CISPEP   3 ILE A  384    PRO A  385          0         6.29                     
SITE     1 AC1 22 VAL A 173  ILE A 176  TYR A 177  LEU A 181                    
SITE     2 AC1 22 ARG A 210  GLY A 211  SER A 212  THR A 214                    
SITE     3 AC1 22 ARG A 218  THR A 237  ASP A 256  VAL A 257                    
SITE     4 AC1 22 LEU A 259  GLY A 273  SER A 277  ARG A 279                    
SITE     5 AC1 22 HOH A 516  HOH A 551  HOH A 563  HOH A 681                    
SITE     6 AC1 22 HOH B1113  HOH B1116                                          
SITE     1 AC2  7 ASP B 452  VAL B 453  GLU B 455  ASP B 469                    
SITE     2 AC2  7 GLN B 470  GLU B 473  HOH B1103                               
SITE     1 AC3 12 SER A  51  ASN A  53  SER A  55  VAL A 257                    
SITE     2 AC3 12 HIS A 258  ASP A 261  HOH A 571  HOH A 581                    
SITE     3 AC3 12 HOH A 585  HOH A 637  HOH A 668  HOH A 680                    
SITE     1 AC4  7 GLY A 120  ARG A 121  ASN A 204  ASP A 233                    
SITE     2 AC4  7 TYR A 265  HOH A 590  HOH A 612                               
SITE     1 AC5  3 LYS A 306  ASN A 373  HOH A 742                               
CRYST1   70.951   74.072   83.583  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      0.014094  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013500  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011964        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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