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Database: PDB
Entry: 5KY3
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HEADER    TRANSFERASE                             21-JUL-16   5KY3              
TITLE     MOUSE POFUT1 IN COMPLEX WITH MOUSE FACTOR VII EGF1 MUTANT (T101A) AND 
TITLE    2 GDP-FUCOSE                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GDP-FUCOSE PROTEIN O-FUCOSYLTRANSFERASE 1;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PEPTIDE-O-FUCOSYLTRANSFERASE 1,O-FUCT-1;                    
COMPND   5 EC: 2.4.1.221;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: COAGULATION FACTOR VII;                                    
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: SERUM PROTHROMBIN CONVERSION ACCELERATOR;                   
COMPND  11 EC: 3.4.21.21;                                                       
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: POFUT1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PB-T-PAF;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: MOUSE;                                              
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 GENE: F7, CF7;                                                       
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GLYCOSYLTRANSFERASE, TRANSFERASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.LI,J.M.RINI                                                         
REVDAT   3   28-JUN-17 5KY3    1       JRNL                                     
REVDAT   2   31-MAY-17 5KY3    1       JRNL                                     
REVDAT   1   17-MAY-17 5KY3    0                                                
JRNL        AUTH   Z.LI,K.HAN,J.E.PAK,M.SATKUNARAJAH,D.ZHOU,J.M.RINI            
JRNL        TITL   RECOGNITION OF EGF-LIKE DOMAINS BY THE NOTCH-MODIFYING       
JRNL        TITL 2 O-FUCOSYLTRANSFERASE POFUT1.                                 
JRNL        REF    NAT. CHEM. BIOL.              V.  13   757 2017              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   28530709                                                     
JRNL        DOI    10.1038/NCHEMBIO.2381                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.53 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) : 1.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.13                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 58040                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.148                           
REMARK   3   FREE R VALUE                     : 0.164                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2914                            
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 47.1497 -  4.2202    0.99     2866   135  0.1466 0.1402        
REMARK   3     2  4.2202 -  3.3500    1.00     2729   166  0.1322 0.1423        
REMARK   3     3  3.3500 -  2.9266    1.00     2696   142  0.1461 0.1590        
REMARK   3     4  2.9266 -  2.6590    1.00     2673   153  0.1460 0.1652        
REMARK   3     5  2.6590 -  2.4685    1.00     2669   157  0.1381 0.1775        
REMARK   3     6  2.4685 -  2.3229    1.00     2673   152  0.1361 0.1398        
REMARK   3     7  2.3229 -  2.2066    1.00     2639   144  0.1405 0.1469        
REMARK   3     8  2.2066 -  2.1105    1.00     2679   113  0.1397 0.1750        
REMARK   3     9  2.1105 -  2.0293    1.00     2648   146  0.1435 0.1734        
REMARK   3    10  2.0293 -  1.9593    1.00     2671   124  0.1475 0.1735        
REMARK   3    11  1.9593 -  1.8980    1.00     2656   132  0.1527 0.2037        
REMARK   3    12  1.8980 -  1.8437    1.00     2595   152  0.1549 0.1719        
REMARK   3    13  1.8437 -  1.7952    1.00     2656   134  0.1540 0.1937        
REMARK   3    14  1.7952 -  1.7514    1.00     2656   124  0.1552 0.1731        
REMARK   3    15  1.7514 -  1.7116    1.00     2633   144  0.1648 0.1844        
REMARK   3    16  1.7116 -  1.6752    1.00     2579   152  0.1672 0.2105        
REMARK   3    17  1.6752 -  1.6417    1.00     2662   133  0.1842 0.2080        
REMARK   3    18  1.6417 -  1.6107    0.99     2618   131  0.1938 0.2108        
REMARK   3    19  1.6107 -  1.5819    0.97     2514   144  0.2021 0.2200        
REMARK   3    20  1.5819 -  1.5551    0.92     2460   112  0.2185 0.2578        
REMARK   3    21  1.5551 -  1.5300    0.83     2154   124  0.2494 0.2966        
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)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.320           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.43                          
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      :  0.007           3313                                  
REMARK   3   ANGLE     :  1.117           4545                                  
REMARK   3   CHIRALITY :  0.058            486                                  
REMARK   3   PLANARITY :  0.007            580                                  
REMARK   3   DIHEDRAL  : 12.659           1976                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 121 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2855  38.4833  24.0996              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1533 T22:   0.1383                                     
REMARK   3      T33:   0.1448 T12:  -0.0033                                     
REMARK   3      T13:   0.0023 T23:  -0.0414                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1564 L22:   1.4463                                     
REMARK   3      L33:   1.1323 L12:   0.1395                                     
REMARK   3      L13:   0.2084 L23:   0.7639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0146 S12:  -0.0399 S13:   0.0614                       
REMARK   3      S21:   0.0125 S22:  -0.1491 S23:   0.1738                       
REMARK   3      S31:   0.0239 S32:  -0.1270 S33:   0.1360                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 122 THROUGH 186 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9781  53.7329  19.1533              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3052 T22:   0.1582                                     
REMARK   3      T33:   0.2360 T12:   0.0201                                     
REMARK   3      T13:  -0.0606 T23:  -0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7193 L22:   1.8759                                     
REMARK   3      L33:   1.0602 L12:   0.4521                                     
REMARK   3      L13:   0.5171 L23:   0.7939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1634 S12:   0.1104 S13:   0.5325                       
REMARK   3      S21:  -0.3537 S22:  -0.0781 S23:   0.2305                       
REMARK   3      S31:  -0.4362 S32:  -0.0430 S33:   0.1555                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 187 THROUGH 259 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8704  29.9793  15.0364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1193 T22:   0.1393                                     
REMARK   3      T33:   0.1191 T12:   0.0056                                     
REMARK   3      T13:  -0.0010 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7668 L22:   1.8846                                     
REMARK   3      L33:   1.4605 L12:  -0.1920                                     
REMARK   3      L13:  -0.1732 L23:   1.1475                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0238 S12:   0.0802 S13:  -0.0378                       
REMARK   3      S21:  -0.0493 S22:  -0.0607 S23:   0.0216                       
REMARK   3      S31:  -0.0248 S32:  -0.0629 S33:   0.0695                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 260 THROUGH 384 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8034  19.9927   4.5101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1329 T22:   0.1703                                     
REMARK   3      T33:   0.1339 T12:  -0.0016                                     
REMARK   3      T13:   0.0058 T23:  -0.0343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3269 L22:   1.5158                                     
REMARK   3      L33:   2.4847 L12:  -0.7204                                     
REMARK   3      L13:  -0.2311 L23:   0.9745                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0118 S12:   0.3754 S13:  -0.1404                       
REMARK   3      S21:  -0.1191 S22:  -0.0962 S23:   0.0052                       
REMARK   3      S31:  -0.0790 S32:   0.0408 S33:   0.0602                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 90 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2655  45.3570   3.3756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5876 T22:   0.4181                                     
REMARK   3      T33:   0.5423 T12:  -0.0435                                     
REMARK   3      T13:   0.0457 T23:   0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0775 L22:   5.5761                                     
REMARK   3      L33:   5.9908 L12:   0.4907                                     
REMARK   3      L13:  -2.8448 L23:  -2.0122                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0399 S12:   0.6212 S13:   0.6911                       
REMARK   3      S21:  -0.7594 S22:   0.0455 S23:  -0.6565                       
REMARK   3      S31:  -0.6678 S32:   0.4401 S33:   0.0423                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 113 THROUGH 126 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.4943  42.0135  -0.1180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8178 T22:   0.4332                                     
REMARK   3      T33:   0.4699 T12:  -0.0600                                     
REMARK   3      T13:  -0.1589 T23:   0.0202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7356 L22:   6.0281                                     
REMARK   3      L33:   6.2389 L12:   4.8878                                     
REMARK   3      L13:   1.1290 L23:   2.7470                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0510 S12:   1.1212 S13:   0.5929                       
REMARK   3      S21:  -1.7322 S22:   0.5504 S23:   0.8174                       
REMARK   3      S31:  -0.1442 S32:  -0.1367 S33:   0.3641                       
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 5KY3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222900.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
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   : 59408                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.526                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
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   (%): 42.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG2000 MME, 50 MM TRIS PH 8.5,      
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       26.07500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.03050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.43450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.03050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.07500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.43450            
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: 2590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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    30                                                      
REMARK 465     ASP B    87                                                      
REMARK 465     GLY B    88                                                      
REMARK 465     ASP B    89                                                      
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     ALA A  31    N    CA   CB                                        
REMARK 470     LYS A 142    CG   CD   CE   NZ                                   
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
REMARK 470     LYS A 166    CE   NZ                                             
REMARK 470     GLN A 203    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 251    CG   CD   CE   NZ                                   
REMARK 470     MET A 256    CG   SD   CE                                        
REMARK 470     LEU A 257    CG   CD1  CD2                                       
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     ASP A 259    CG   OD1  OD2                                       
REMARK 470     THR A 261    OG1  CG2                                            
REMARK 470     ARG A 277    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 278    OG                                                  
REMARK 470     THR A 279    OG1  CG2                                            
REMARK 470     LYS A 329    CG   CD   CE   NZ                                   
REMARK 470     ASP A 330    CG   OD1  OD2                                       
REMARK 470     LYS A 331    CG   CD   CE   NZ                                   
REMARK 470     ARG A 333    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  90    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 106    CG   CD1  CD2                                       
REMARK 470     LYS B 107    CG   CD   CE   NZ                                   
REMARK 470     LEU B 115    CG   CD1  CD2                                       
REMARK 470     LYS B 124    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   817     O    HOH A   826              2.03            
REMARK 500   O    HOH A   713     O    HOH A   818              2.09            
REMARK 500   O    HOH A   831     O    HOH A   836              2.09            
REMARK 500   O    HOH A   513     O    HOH A   575              2.10            
REMARK 500   O    HOH A   802     O    HOH A   804              2.16            
REMARK 500   O    HOH A   654     O    HOH A   849              2.17            
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    MET A 267     -128.78     58.10                                   
REMARK 500    SER A 317     -108.50   -159.90                                   
REMARK 500    ASP A 330       -9.51     94.50                                   
REMARK 500    MET A 383       86.65   -152.47                                   
REMARK 500    LEU B 106     -137.38     59.34                                   
REMARK 500    SER B 108     -142.12   -135.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 890        DISTANCE =  5.97 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GFB A 404                 
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 67                                                         
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 165                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KHX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KXQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KY0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KY2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KY4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KY5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KY7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KY8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KY9   RELATED DB: PDB                                   
DBREF  5KY3 A   33   384  UNP    Q91ZW2   OFUT1_MOUSE     33    384             
DBREF  5KY3 B   87   126  UNP    P70375   FA7_MOUSE       87    126             
SEQADV 5KY3 GLY A   30  UNP  Q91ZW2              EXPRESSION TAG                 
SEQADV 5KY3 ALA A   31  UNP  Q91ZW2              EXPRESSION TAG                 
SEQADV 5KY3 PRO A   32  UNP  Q91ZW2              EXPRESSION TAG                 
SEQADV 5KY3 ALA B  101  UNP  P70375    THR   101 ENGINEERED MUTATION            
SEQRES   1 A  355  GLY ALA PRO SER TRP ASP LEU ALA GLY TYR LEU LEU TYR          
SEQRES   2 A  355  CYS PRO CYS MET GLY ARG PHE GLY ASN GLN ALA ASP HIS          
SEQRES   3 A  355  PHE LEU GLY SER LEU ALA PHE ALA LYS LEU LEU ASN ARG          
SEQRES   4 A  355  THR LEU ALA VAL PRO PRO TRP ILE GLU TYR GLN HIS HIS          
SEQRES   5 A  355  LYS PRO PRO PHE THR ASN LEU HIS VAL SER TYR GLN LYS          
SEQRES   6 A  355  TYR PHE LYS LEU GLU PRO LEU GLN ALA TYR HIS ARG VAL          
SEQRES   7 A  355  VAL SER LEU GLU ASP PHE MET GLU ASN LEU ALA PRO SER          
SEQRES   8 A  355  HIS TRP PRO PRO GLU LYS ARG VAL ALA TYR CYS PHE GLU          
SEQRES   9 A  355  VAL ALA ALA GLN ARG SER PRO ASP LYS LYS THR CYS PRO          
SEQRES  10 A  355  MET LYS GLU GLY ASN PRO PHE GLY PRO PHE TRP ASP GLN          
SEQRES  11 A  355  PHE HIS VAL SER PHE ASN LYS SER GLU LEU PHE THR GLY          
SEQRES  12 A  355  ILE SER PHE SER ALA SER TYR LYS GLU GLN TRP THR GLN          
SEQRES  13 A  355  ARG PHE PRO ALA LYS GLU HIS PRO VAL LEU ALA LEU PRO          
SEQRES  14 A  355  GLY ALA PRO ALA GLN PHE PRO VAL LEU GLU GLU HIS ARG          
SEQRES  15 A  355  GLU LEU GLN LYS TYR MET VAL TRP SER ASP GLU MET VAL          
SEQRES  16 A  355  ARG THR GLY GLU ALA LEU ILE SER ALA HIS LEU VAL ARG          
SEQRES  17 A  355  PRO TYR VAL GLY ILE HIS LEU ARG ILE GLY SER ASP TRP          
SEQRES  18 A  355  LYS ASN ALA CYS ALA MET LEU LYS ASP GLY THR ALA GLY          
SEQRES  19 A  355  SER HIS PHE MET ALA SER PRO GLN CYS VAL GLY TYR SER          
SEQRES  20 A  355  ARG SER THR ALA THR PRO LEU THR MET THR MET CYS LEU          
SEQRES  21 A  355  PRO ASP LEU LYS GLU ILE GLN ARG ALA VAL THR LEU TRP          
SEQRES  22 A  355  VAL ARG ALA LEU ASN ALA ARG SER VAL TYR ILE ALA THR          
SEQRES  23 A  355  ASP SER GLU SER TYR VAL SER GLU ILE GLN GLN LEU PHE          
SEQRES  24 A  355  LYS ASP LYS VAL ARG VAL VAL SER LEU LYS PRO GLU VAL          
SEQRES  25 A  355  ALA GLN ILE ASP LEU TYR ILE LEU GLY GLN ALA ASP HIS          
SEQRES  26 A  355  PHE ILE GLY ASN CYS VAL SER SER PHE THR ALA PHE VAL          
SEQRES  27 A  355  LYS ARG GLU ARG ASP LEU HIS GLY ARG GLN SER SER PHE          
SEQRES  28 A  355  PHE GLY MET ASP                                              
SEQRES   1 B   40  ASP GLY ASP GLN CYS ALA SER ASN PRO CYS GLN ASN GLY          
SEQRES   2 B   40  GLY ALA CYS GLN ASP HIS LEU LYS SER TYR VAL CYS PHE          
SEQRES   3 B   40  CYS LEU LEU ASP PHE GLU GLY ARG ASN CYS GLU LYS SER          
SEQRES   4 B   40  LYS                                                          
HET    NAG  A 401      14                                                       
HET    NAG  A 402      14                                                       
HET    GOL  A 403       6                                                       
HET    GFB  A 404      66                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     GOL GLYCEROL                                                         
HETNAM     GFB GUANOSINE-5'-DIPHOSPHATE-BETA-L-FUCOPYRANOSE                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  GFB    C16 H25 N5 O15 P2                                            
FORMUL   7  HOH   *407(H2 O)                                                    
HELIX    1 AA1 ARG A   48  ASN A   67  1                                  20    
HELIX    2 AA2 SER A   91  PHE A   96  1                                   6    
HELIX    3 AA3 LEU A   98  TYR A  104  5                                   7    
HELIX    4 AA4 LEU A  110  LEU A  117  1                                   8    
HELIX    5 AA5 LEU A  117  TRP A  122  1                                   6    
HELIX    6 AA6 PRO A  123  LYS A  126  5                                   4    
HELIX    7 AA7 GLU A  133  GLN A  137  1                                   5    
HELIX    8 AA8 PRO A  152  GLN A  159  1                                   8    
HELIX    9 AA9 SER A  176  SER A  178  5                                   3    
HELIX   10 AB1 TYR A  179  PHE A  187  1                                   9    
HELIX   11 AB2 LEU A  207  MET A  217  5                                  11    
HELIX   12 AB3 SER A  220  LEU A  235  1                                  16    
HELIX   13 AB4 GLY A  247  GLY A  260  1                                  14    
HELIX   14 AB5 SER A  269  GLY A  274  1                                   6    
HELIX   15 AB6 THR A  284  LEU A  289  1                                   6    
HELIX   16 AB7 ASP A  291  ASN A  307  1                                  17    
HELIX   17 AB8 TYR A  320  GLN A  326  1                                   7    
HELIX   18 AB9 VAL A  341  GLN A  351  1                                  11    
HELIX   19 AC1 SER A  361  HIS A  374  1                                  14    
HELIX   20 AC2 GLN B   90  ASN B   94  5                                   5    
SHEET    1 AA1 4 VAL A 107  SER A 109  0                                        
SHEET    2 AA1 4 THR A  69  VAL A  72  1  N  VAL A  72   O  VAL A 108           
SHEET    3 AA1 4 TYR A  39  TYR A  42  1  N  LEU A  40   O  ALA A  71           
SHEET    4 AA1 4 VAL A 194  LEU A 197  1  O  LEU A 195   N  LEU A  41           
SHEET    1 AA2 2 TRP A  75  GLU A  77  0                                        
SHEET    2 AA2 2 LEU A  88  VAL A  90 -1  O  LEU A  88   N  GLU A  77           
SHEET    1 AA3 2 VAL A 128  PHE A 132  0                                        
SHEET    2 AA3 2 LYS A 166  PHE A 170  1  O  GLU A 168   N  ALA A 129           
SHEET    1 AA4 5 ARG A 333  VAL A 335  0                                        
SHEET    2 AA4 5 SER A 310  THR A 315  1  N  VAL A 311   O  VAL A 335           
SHEET    3 AA4 5 TYR A 239  LEU A 244  1  N  LEU A 244   O  ALA A 314           
SHEET    4 AA4 5 HIS A 354  GLY A 357  1  O  HIS A 354   N  GLY A 241           
SHEET    5 AA4 5 SER A 378  PHE A 380  1  O  SER A 379   N  PHE A 355           
SHEET    1 AA5 2 ALA B 101  GLN B 103  0                                        
SHEET    2 AA5 2 VAL B 110  PHE B 112 -1  O  PHE B 112   N  ALA B 101           
SHEET    1 AA6 2 PHE B 117  GLU B 118  0                                        
SHEET    2 AA6 2 LYS B 124  SER B 125 -1  O  LYS B 124   N  GLU B 118           
SSBOND   1 CYS A   43    CYS A   45                          1555   1555  2.00  
SSBOND   2 CYS A  131    CYS A  145                          1555   1555  2.06  
SSBOND   3 CYS A  254    CYS A  288                          1555   1555  2.05  
SSBOND   4 CYS A  272    CYS A  359                          1555   1555  2.04  
SSBOND   5 CYS B   91    CYS B  102                          1555   1555  2.04  
SSBOND   6 CYS B   96    CYS B  111                          1555   1555  2.04  
SSBOND   7 CYS B  113    CYS B  122                          1555   1555  2.05  
LINK         ND2 ASN A  67                 C1  NAG A 401     1555   1555  1.44  
LINK         ND2 ASN A 165                 C1  NAG A 402     1555   1555  1.43  
CISPEP   1 PRO A   83    PRO A   84          0         5.34                     
CISPEP   2 ASN A  151    PRO A  152          0        13.19                     
CISPEP   3 PHE A  204    PRO A  205          0        -2.73                     
CISPEP   4 ARG A  237    PRO A  238          0        -4.25                     
SITE     1 AC1  6 PHE A 170  THR A 171  GLN A 182  ARG A 186                    
SITE     2 AC1  6 HOH A 504  HOH A 778                                          
SITE     1 AC2 26 ARG A  48  PHE A  49  GLY A  50  ASN A  51                    
SITE     2 AC2 26 HIS A 243  ARG A 245  ASP A 249  TRP A 250                    
SITE     3 AC2 26 MET A 267  ALA A 314  THR A 315  ASP A 316                    
SITE     4 AC2 26 PRO A 339  ALA A 342  ASP A 345  SER A 361                    
SITE     5 AC2 26 SER A 362  PHE A 363  HOH A 534  HOH A 617                    
SITE     6 AC2 26 HOH A 732  HOH A 736  HOH A 750  GLY B  99                    
SITE     7 AC2 26 PHE B 112  LEU B 114                                          
SITE     1 AC3 13 ASP A  35  ALA A  37  ASN A  67  ARG A 106                    
SITE     2 AC3 13 GLN A 351  ARG A 376  HOH A 514  HOH A 530                    
SITE     3 AC3 13 HOH A 532  HOH A 540  HOH A 590  HOH A 677                    
SITE     4 AC3 13 HOH A 780                                                     
SITE     1 AC4  4 GLU A 125  ASN A 165  HOH A 584  HOH A 622                    
CRYST1   52.150   66.869  110.061  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      0.019175  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014955  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009086        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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