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Database: PDB
Entry: 5KY8
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HEADER    TRANSFERASE                             21-JUL-16   5KY8              
TITLE     MOUSE POFUT1 IN COMPLEX WITH O-GLUCOSYLATED MOUSE NOTCH1 EGF12 MUTANT 
TITLE    2 (D464G) AND GDP                                                      
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: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: NOTCH 1,MOTCH A,MT14,P300;                                  
COMPND  11 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: NOTCH1, MOTCH;                                                 
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 5KY8    1       JRNL                                     
REVDAT   2   31-MAY-17 5KY8    1       JRNL                                     
REVDAT   1   17-MAY-17 5KY8    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.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.42                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 44211                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2225                            
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 46.4384 -  4.1568    0.97     2757   133  0.1630 0.1822        
REMARK   3     2  4.1568 -  3.2997    0.98     2622   159  0.1580 0.1682        
REMARK   3     3  3.2997 -  2.8826    0.98     2637   139  0.1837 0.2214        
REMARK   3     4  2.8826 -  2.6191    0.99     2606   152  0.1922 0.2027        
REMARK   3     5  2.6191 -  2.4314    0.99     2629   148  0.1927 0.2220        
REMARK   3     6  2.4314 -  2.2880    0.99     2616   154  0.1986 0.2319        
REMARK   3     7  2.2880 -  2.1735    1.00     2628   145  0.1990 0.2271        
REMARK   3     8  2.1735 -  2.0788    1.00     2628   116  0.2069 0.2338        
REMARK   3     9  2.0788 -  1.9988    1.00     2607   138  0.2160 0.2295        
REMARK   3    10  1.9988 -  1.9298    1.00     2638   123  0.2294 0.2559        
REMARK   3    11  1.9298 -  1.8695    1.00     2636   131  0.2389 0.2642        
REMARK   3    12  1.8695 -  1.8161    1.00     2602   143  0.2526 0.2973        
REMARK   3    13  1.8161 -  1.7682    1.00     2605   127  0.2734 0.3260        
REMARK   3    14  1.7682 -  1.7251    1.00     2600   136  0.2867 0.2834        
REMARK   3    15  1.7251 -  1.6859    1.00     2630   138  0.3128 0.3360        
REMARK   3    16  1.6859 -  1.6500    0.99     2545   143  0.3360 0.3654        
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) : 24.720           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.15                          
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      :  0.004           3224                                  
REMARK   3   ANGLE     :  0.776           4402                                  
REMARK   3   CHIRALITY :  0.046            471                                  
REMARK   3   PLANARITY :  0.005            565                                  
REMARK   3   DIHEDRAL  : 15.714           1904                                  
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 33 THROUGH 121 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9828  39.1978  22.5978              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2576 T22:   0.3462                                     
REMARK   3      T33:   0.1943 T12:  -0.0235                                     
REMARK   3      T13:   0.0287 T23:  -0.0757                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4151 L22:   2.7063                                     
REMARK   3      L33:   1.9433 L12:  -0.1159                                     
REMARK   3      L13:  -0.2674 L23:   0.8173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0145 S12:  -0.5020 S13:   0.0333                       
REMARK   3      S21:   0.2274 S22:  -0.1409 S23:   0.2231                       
REMARK   3      S31:   0.0877 S32:   0.1171 S33:   0.1463                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 122 THROUGH 234 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4240  45.8454  18.7842              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2547 T22:   0.2634                                     
REMARK   3      T33:   0.1685 T12:  -0.0433                                     
REMARK   3      T13:   0.0050 T23:  -0.0801                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2677 L22:   3.1062                                     
REMARK   3      L33:   1.3670 L12:  -0.2719                                     
REMARK   3      L13:  -0.4509 L23:   0.7816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0069 S12:  -0.3124 S13:   0.2668                       
REMARK   3      S21:   0.0614 S22:   0.0050 S23:   0.0020                       
REMARK   3      S31:  -0.2072 S32:   0.1447 S33:   0.0285                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 235 THROUGH 384 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7623  21.1268   3.8743              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1969 T22:   0.1643                                     
REMARK   3      T33:   0.3097 T12:  -0.0005                                     
REMARK   3      T13:   0.0359 T23:  -0.0551                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3843 L22:   3.2658                                     
REMARK   3      L33:   2.3200 L12:  -0.7265                                     
REMARK   3      L13:  -1.6673 L23:   1.2215                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2255 S12:   0.1538 S13:  -0.7375                       
REMARK   3      S21:  -0.0402 S22:  -0.1005 S23:   0.1193                       
REMARK   3      S31:   0.0888 S32:   0.0052 S33:   0.0741                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 453 THROUGH 458 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7130  50.4926   5.6616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5588 T22:   0.3704                                     
REMARK   3      T33:   0.8051 T12:  -0.1161                                     
REMARK   3      T13:   0.1340 T23:  -0.0448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0643 L22:   1.2404                                     
REMARK   3      L33:   6.4246 L12:   2.9135                                     
REMARK   3      L13:  -5.0543 L23:  -2.4064                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3589 S12:  -0.2625 S13:   0.7923                       
REMARK   3      S21:  -1.1214 S22:  -0.1862 S23:  -1.7609                       
REMARK   3      S31:  -1.2185 S32:   1.1264 S33:  -0.1306                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 459 THROUGH 477 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2840  44.9278   1.7021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5017 T22:   0.3321                                     
REMARK   3      T33:   0.4858 T12:   0.0631                                     
REMARK   3      T13:   0.0486 T23:   0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3417 L22:   1.9455                                     
REMARK   3      L33:   5.5155 L12:  -2.5545                                     
REMARK   3      L13:  -1.8716 L23:   0.6247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5367 S12:   0.1690 S13:   0.9318                       
REMARK   3      S21:  -0.8126 S22:  -0.5386 S23:  -0.2289                       
REMARK   3      S31:  -0.6236 S32:   0.0320 S33:  -0.0375                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 478 THROUGH 491 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8576  41.6919  -1.6326              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6126 T22:   0.6035                                     
REMARK   3      T33:   0.5775 T12:   0.0618                                     
REMARK   3      T13:  -0.2836 T23:  -0.0388                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5726 L22:   2.7036                                     
REMARK   3      L33:   7.1139 L12:  -0.7536                                     
REMARK   3      L13:  -0.7659 L23:  -1.9902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4258 S12:   1.0144 S13:   0.4953                       
REMARK   3      S21:  -1.3869 S22:   0.1007 S23:   1.5207                       
REMARK   3      S31:  -0.4185 S32:  -1.2459 S33:   0.2032                       
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 5KY8 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_1000222904.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-13                          
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   : 44218                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.12700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.330                              
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   (%): 39.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
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       25.77000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.41500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.41500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.77000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.95000            
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: 3190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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     ALA A    31                                                      
REMARK 465     PRO A    32                                                      
REMARK 465     ASP B   452                                                      
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  33    OG                                                  
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
REMARK 470     LYS A 166    CG   CD   CE   NZ                                   
REMARK 470     GLU A 181    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 190    CG   CD   CE   NZ                                   
REMARK 470     LYS A 251    CG   CD   CE   NZ                                   
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     ASP A 259    CG   OD1  OD2                                       
REMARK 470     LYS A 293    CG   CD   CE   NZ                                   
REMARK 470     GLN A 326    CG   CD   OE1  NE2                                  
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     VAL B 453    CG1  CG2                                            
REMARK 470     GLN B 470    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    VAL A   273     HG1  THR A   279              1.57            
REMARK 500   OD2  ASP A   141     H    LYS A   143              1.58            
REMARK 500   O    HOH A   683     O    HOH A   724              2.19            
REMARK 500   ND2  ASN A    67     O5   NAG A   401              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 272   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A 246       13.34   -141.39                                   
REMARK 500    MET A 267     -116.82     46.68                                   
REMARK 500    SER A 317     -118.75   -154.98                                   
REMARK 500    ASP A 330       -3.18     93.96                                   
REMARK 500    MET A 383       85.60   -154.01                                   
REMARK 500    GLU B 473     -177.12   -176.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
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: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide BGC B 1001        
REMARK 800  bound to SER B 458                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KXH   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: 5KY3   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: 5KY9   RELATED DB: PDB                                   
DBREF  5KY8 A   33   384  UNP    Q91ZW2   OFUT1_MOUSE     33    384             
DBREF  5KY8 B  452   491  UNP    Q01705   NOTC1_MOUSE    452    491             
SEQADV 5KY8 GLY A   30  UNP  Q91ZW2              EXPRESSION TAG                 
SEQADV 5KY8 ALA A   31  UNP  Q91ZW2              EXPRESSION TAG                 
SEQADV 5KY8 PRO A   32  UNP  Q91ZW2              EXPRESSION TAG                 
SEQADV 5KY8 GLY B  464  UNP  Q01705    ASP   464 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 VAL ASN GLU CYS ILE SER ASN PRO CYS GLN ASN GLY          
SEQRES   2 B   40  ALA THR CYS LEU ASP GLN ILE GLY GLU PHE GLN CYS ILE          
SEQRES   3 B   40  CYS MET PRO GLY TYR GLU GLY VAL TYR CYS GLU ILE ASN          
SEQRES   4 B   40  THR                                                          
HET    NAG  A 401      28                                                       
HET    GDP  A 402      38                                                       
HET    BGC  B1001      21                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     BGC BETA-D-GLUCOSE                                                   
FORMUL   3  NAG    C8 H15 N O6                                                  
FORMUL   4  GDP    C10 H15 N5 O11 P2                                            
FORMUL   5  BGC    C6 H12 O6                                                    
FORMUL   6  HOH   *271(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  ASP A  259  1                                  13    
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 ASN B  454  ASN B  459  5                                   6    
SHEET    1 AA1 4 VAL A 107  SER A 109  0                                        
SHEET    2 AA1 4 THR A  69  VAL A  72  1  N  LEU A  70   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  SER A 336  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 THR B 466  ASP B 469  0                                        
SHEET    2 AA5 2 PHE B 474  ILE B 477 -1  O  ILE B 477   N  THR B 466           
SHEET    1 AA6 2 TYR B 482  GLU B 483  0                                        
SHEET    2 AA6 2 ILE B 489  ASN B 490 -1  O  ILE B 489   N  GLU B 483           
SSBOND   1 CYS A   43    CYS A   45                          1555   1555  2.04  
SSBOND   2 CYS A  131    CYS A  145                          1555   1555  2.03  
SSBOND   3 CYS A  254    CYS A  288                          1555   1555  2.03  
SSBOND   4 CYS A  272    CYS A  359                          1555   1555  2.05  
SSBOND   5 CYS B  456    CYS B  467                          1555   1555  1.92  
SSBOND   6 CYS B  461    CYS B  476                          1555   1555  2.03  
SSBOND   7 CYS B  478    CYS B  487                          1555   1555  2.03  
LINK         ND2 ASN A  67                 C1  NAG A 401     1555   1555  1.40  
LINK         OG  SER B 458                 C1  BGC B1001     1555   1555  1.48  
CISPEP   1 PRO A   83    PRO A   84          0         4.02                     
CISPEP   2 ASN A  151    PRO A  152          0         4.99                     
CISPEP   3 PHE A  204    PRO A  205          0        -1.92                     
CISPEP   4 ARG A  237    PRO A  238          0        -2.00                     
SITE     1 AC1 18 ARG A  48  PHE A  49  GLY A  50  ASN A  51                    
SITE     2 AC1 18 HIS A 243  ARG A 245  TRP A 250  ALA A 314                    
SITE     3 AC1 18 THR A 315  ASP A 316  PRO A 339  ASP A 345                    
SITE     4 AC1 18 SER A 361  SER A 362  PHE A 363  HOH A 517                    
SITE     5 AC1 18 HOH A 577  HOH A 607                                          
SITE     1 AC2 13 ASP A  35  ALA A  37  ASN A  67  ARG A 106                    
SITE     2 AC2 13 GLN A 351  ALA A 352  ASP A 353  ARG A 371                    
SITE     3 AC2 13 GLY A 375  ARG A 376  HOH A 505  HOH A 581                    
SITE     4 AC2 13 HOH A 602                                                     
SITE     1 AC3  5 ARG A 138  GLU B 455  SER B 458  PHE B 474                    
SITE     2 AC3  5 TYR B 486                                                     
CRYST1   51.540   65.900  106.830  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      0.019402  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015175  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009361        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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