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Database: PDB
Entry: 5KY4
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Original site: 5KY4 
HEADER    TRANSFERASE                             21-JUL-16   5KY4              
TITLE     MOUSE POFUT1 IN COMPLEX WITH MOUSE NOTCH1 EGF26 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 5KY4    1       JRNL                                     
REVDAT   2   31-MAY-17 5KY4    1       JRNL                                     
REVDAT   1   17-MAY-17 5KY4    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.    1.47 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) : 1.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.02                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 62128                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.168                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3126                            
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 47.0467 -  4.1233    0.99     3057   143  0.1539 0.1519        
REMARK   3     2  4.1233 -  3.2730    1.00     2894   172  0.1379 0.1523        
REMARK   3     3  3.2730 -  2.8594    1.00     2872   155  0.1458 0.1538        
REMARK   3     4  2.8594 -  2.5979    1.00     2856   162  0.1438 0.1394        
REMARK   3     5  2.5979 -  2.4117    1.00     2824   167  0.1359 0.1787        
REMARK   3     6  2.4117 -  2.2696    1.00     2816   164  0.1311 0.1404        
REMARK   3     7  2.2696 -  2.1559    1.00     2856   137  0.1378 0.1514        
REMARK   3     8  2.1559 -  2.0621    1.00     2844   139  0.1378 0.1474        
REMARK   3     9  2.0621 -  1.9827    1.00     2827   146  0.1418 0.1635        
REMARK   3    10  1.9827 -  1.9142    1.00     2842   127  0.1455 0.1650        
REMARK   3    11  1.9142 -  1.8544    1.00     2782   159  0.1539 0.1743        
REMARK   3    12  1.8544 -  1.8014    1.00     2826   143  0.1608 0.2314        
REMARK   3    13  1.8014 -  1.7540    1.00     2828   142  0.1580 0.1916        
REMARK   3    14  1.7540 -  1.7112    1.00     2815   156  0.1657 0.1747        
REMARK   3    15  1.7112 -  1.6723    1.00     2777   158  0.1667 0.2232        
REMARK   3    16  1.6723 -  1.6367    1.00     2811   138  0.1840 0.1841        
REMARK   3    17  1.6367 -  1.6039    0.99     2806   146  0.2137 0.2334        
REMARK   3    18  1.6039 -  1.5737    0.97     2719   148  0.2236 0.2915        
REMARK   3    19  1.5737 -  1.5456    0.93     2594   135  0.2500 0.2434        
REMARK   3    20  1.5456 -  1.5194    0.83     2316   119  0.2826 0.2909        
REMARK   3    21  1.5194 -  1.4948    0.67     1867   104  0.3101 0.2904        
REMARK   3    22  1.4948 -  1.4718    0.42     1173    66  0.3333 0.3230        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.430           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.52                          
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           3329                                  
REMARK   3   ANGLE     :  1.014           4555                                  
REMARK   3   CHIRALITY :  0.073            483                                  
REMARK   3   PLANARITY :  0.007            589                                  
REMARK   3   DIHEDRAL  : 19.710           1225                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 48 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7904  43.5144  26.1458              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1575 T22:   0.1317                                     
REMARK   3      T33:   0.1651 T12:  -0.0088                                     
REMARK   3      T13:  -0.0050 T23:  -0.0299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6476 L22:   2.3133                                     
REMARK   3      L33:   6.4081 L12:   0.5784                                     
REMARK   3      L13:   2.1391 L23:   3.6690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0389 S12:  -0.1443 S13:   0.1536                       
REMARK   3      S21:   0.0691 S22:  -0.2278 S23:   0.1756                       
REMARK   3      S31:   0.0245 S32:  -0.2964 S33:   0.2195                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 49 THROUGH 136 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6901  39.9138  23.6682              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1424 T22:   0.1327                                     
REMARK   3      T33:   0.1608 T12:   0.0103                                     
REMARK   3      T13:  -0.0141 T23:  -0.0603                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8980 L22:   1.3852                                     
REMARK   3      L33:   1.4526 L12:   0.3754                                     
REMARK   3      L13:   0.4763 L23:   0.8202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0505 S12:  -0.1055 S13:   0.1733                       
REMARK   3      S21:  -0.0042 S22:  -0.1796 S23:   0.2391                       
REMARK   3      S31:  -0.0762 S32:  -0.2163 S33:   0.1281                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 186 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0925  52.6306  18.6661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3536 T22:   0.2020                                     
REMARK   3      T33:   0.2799 T12:   0.0085                                     
REMARK   3      T13:  -0.0900 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3355 L22:   1.7657                                     
REMARK   3      L33:   0.8303 L12:   0.7199                                     
REMARK   3      L13:   1.0839 L23:   1.0405                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2290 S12:   0.1992 S13:   0.6754                       
REMARK   3      S21:  -0.3428 S22:  -0.0942 S23:   0.3054                       
REMARK   3      S31:  -0.4714 S32:  -0.0214 S33:   0.2166                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 187 THROUGH 234 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0929  33.1449  20.9885              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1049 T22:   0.1112                                     
REMARK   3      T33:   0.1158 T12:  -0.0053                                     
REMARK   3      T13:  -0.0125 T23:   0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4957 L22:   2.2909                                     
REMARK   3      L33:   1.5913 L12:  -0.1382                                     
REMARK   3      L13:   0.0763 L23:   1.2706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0383 S12:  -0.0584 S13:   0.0612                       
REMARK   3      S21:   0.0616 S22:  -0.0064 S23:   0.0209                       
REMARK   3      S31:  -0.0099 S32:  -0.0158 S33:   0.0276                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 235 THROUGH 384 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0391  20.2392   3.9670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0851 T22:   0.1134                                     
REMARK   3      T33:   0.0882 T12:  -0.0048                                     
REMARK   3      T13:   0.0037 T23:  -0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8347 L22:   1.8929                                     
REMARK   3      L33:   3.2616 L12:  -0.4328                                     
REMARK   3      L13:  -0.2583 L23:   1.3933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0114 S12:   0.3634 S13:  -0.0723                       
REMARK   3      S21:  -0.1302 S22:  -0.0762 S23:   0.0001                       
REMARK   3      S31:  -0.0999 S32:  -0.0021 S33:   0.0601                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 969 THROUGH 990 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.1696  45.3368   3.7932              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6718 T22:   0.3798                                     
REMARK   3      T33:   0.4719 T12:  -0.1519                                     
REMARK   3      T13:  -0.0315 T23:   0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8418 L22:   6.2601                                     
REMARK   3      L33:   3.7159 L12:  -0.4861                                     
REMARK   3      L13:   0.6379 L23:  -2.5545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0850 S12:   0.3106 S13:   0.8122                       
REMARK   3      S21:  -0.6603 S22:  -0.2714 S23:  -0.6962                       
REMARK   3      S31:  -1.5605 S32:   0.8585 S33:   0.2568                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 991 THROUGH 1004 )                
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2968  41.5360   0.1317              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6415 T22:   0.3491                                     
REMARK   3      T33:   0.3934 T12:   0.1435                                     
REMARK   3      T13:  -0.1810 T23:   0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1617 L22:   3.4486                                     
REMARK   3      L33:   4.7905 L12:  -1.3688                                     
REMARK   3      L13:   1.4716 L23:  -1.9028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0343 S12:   0.6114 S13:   0.5714                       
REMARK   3      S21:  -0.9787 S22:  -0.0290 S23:   0.7967                       
REMARK   3      S31:  -0.8379 S32:  -0.4354 S33:   0.0181                       
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 5KY4 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_1000222901.                                   
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   : 65598                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.470                              
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) : 0.13400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.21800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
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       25.96000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.45500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.18600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.45500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.96000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.18600            
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: 4370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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     ASN B   965                                                      
REMARK 465     THR B   966                                                      
REMARK 465     PRO B   967                                                      
REMARK 465     ASP B   968                                                      
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     GLN A 137    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 138    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 142    CG   CD   CE   NZ                                   
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
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     THR A 281    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     GLU B 971    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 984    CG1  CG2  CD1                                       
REMARK 470     ASN B 985    CG   OD1  ND2                                       
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   HG   SER A   336     O    HOH A   501              1.30            
REMARK 500   O    HOH A   511     O    HOH A   681              1.79            
REMARK 500   O    HOH A   661     O    HOH A   805              1.98            
REMARK 500   O    HOH A   798     O    HOH A   845              2.00            
REMARK 500   OG   SER A   336     O    HOH A   501              2.07            
REMARK 500   O    HOH A   681     O    HOH A   782              2.10            
REMARK 500   O    HOH A   510     O    HOH A   825              2.12            
REMARK 500   O    HOH A   781     O    HOH A   782              2.14            
REMARK 500   O    HOH A   618     O    HOH A   872              2.17            
REMARK 500   O    HOH A   520     O    HOH A   557              2.18            
REMARK 500   O    HOH A   567     O    HOH A   811              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   794     O    HOH A   834     4555     1.88            
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    PRO A 152   C   -  N   -  CD  ANGL. DEV. =  13.6 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    MET A 267     -125.16     46.72                                   
REMARK 500    SER A 317     -106.19   -156.29                                   
REMARK 500    ASP A 330       -1.18     82.04                                   
REMARK 500    ASN B 985       17.13   -140.35                                   
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 893        DISTANCE =  5.88 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A  402                                                       
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 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
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: AC6                                                 
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: 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: 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  5KY4 A   33   384  UNP    Q91ZW2   OFUT1_MOUSE     33    384             
DBREF  5KY4 B  965  1004  UNP    Q01705   NOTC1_MOUSE    925    964             
SEQADV 5KY4 GLY A   30  UNP  Q91ZW2              EXPRESSION TAG                 
SEQADV 5KY4 ALA A   31  UNP  Q91ZW2              EXPRESSION TAG                 
SEQADV 5KY4 PRO A   32  UNP  Q91ZW2              EXPRESSION TAG                 
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  ASN THR PRO ASP CYS THR GLU SER SER CYS PHE ASN GLY          
SEQRES   2 B   40  GLY THR CYS VAL ASP GLY ILE ASN SER PHE THR CYS LEU          
SEQRES   3 B   40  CYS PRO PRO GLY PHE THR GLY SER TYR CYS GLN TYR ASP          
SEQRES   4 B   40  VAL                                                          
HET    NAG  A 401      14                                                       
HET    NAG  A 402      13                                                       
HET    GDP  A 403      28                                                       
HET    PGO  A 404       5                                                       
HET    PGO  A 405       5                                                       
HET    PGO  A 406       5                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     PGO S-1,2-PROPANEDIOL                                                
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   5  GDP    C10 H15 N5 O11 P2                                            
FORMUL   6  PGO    3(C3 H8 O2)                                                  
FORMUL   9  HOH   *406(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  ARG A  138  1                                   6    
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    
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 THR B 979  ASP B 982  0                                        
SHEET    2 AA5 2 PHE B 987  LEU B 990 -1  O  THR B 988   N  VAL B 981           
SHEET    1 AA6 2 PHE B 995  THR B 996  0                                        
SHEET    2 AA6 2 TYR B1002  ASP B1003 -1  O  TYR B1002   N  THR B 996           
SSBOND   1 CYS A   43    CYS A   45                          1555   1555  2.03  
SSBOND   2 CYS A  131    CYS A  145                          1555   1555  2.03  
SSBOND   3 CYS A  254    CYS A  288                          1555   1555  2.04  
SSBOND   4 CYS A  272    CYS A  359                          1555   1555  2.05  
SSBOND   5 CYS B  969    CYS B  980                          1555   1555  2.02  
SSBOND   6 CYS B  974    CYS B  989                          1555   1555  2.05  
SSBOND   7 CYS B  991    CYS B 1000                          1555   1555  2.05  
LINK         ND2 ASN A  67                 C1  NAG A 401     1555   1555  1.45  
LINK         ND2 ASN A 165                 C1  NAG A 402     1555   1555  1.44  
CISPEP   1 PRO A   83    PRO A   84          0         4.98                     
CISPEP   2 ASN A  151    PRO A  152          0         6.23                     
CISPEP   3 PHE A  204    PRO A  205          0        -4.58                     
CISPEP   4 ARG A  237    PRO A  238          0        -2.58                     
SITE     1 AC1 23 ARG A  48  PHE A  49  GLY A  50  ASN A  51                    
SITE     2 AC1 23 HIS A 243  ARG A 245  TRP A 250  ALA A 314                    
SITE     3 AC1 23 THR A 315  ASP A 316  PRO A 339  ALA A 342                    
SITE     4 AC1 23 ASP A 345  SER A 361  SER A 362  PHE A 363                    
SITE     5 AC1 23 HOH A 520  HOH A 546  HOH A 557  HOH A 649                    
SITE     6 AC1 23 HOH A 682  HOH A 723  HOH A 735                               
SITE     1 AC2  8 ARG A  48  ARG A 245  ASP A 249  HOH A 546                    
SITE     2 AC2  8 GLY B 977  THR B 979  LEU B 990  PRO B 992                    
SITE     1 AC3  5 LYS A  64  ASN A  67  HIS A 105  HOH A 593                    
SITE     2 AC3  5 HOH A 781                                                     
SITE     1 AC4  5 PHE A 170  THR A 171  ARG A 186  HOH A 504                    
SITE     2 AC4  5 HOH A 731                                                     
SITE     1 AC5 15 ASP A  35  ALA A  37  ASN A  67  ARG A 106                    
SITE     2 AC5 15 GLN A 351  ARG A 376  HOH A 508  HOH A 511                    
SITE     3 AC5 15 HOH A 522  HOH A 556  HOH A 571  HOH A 681                    
SITE     4 AC5 15 HOH A 694  HOH A 781  HOH A 782                               
SITE     1 AC6  1 ASN A 165                                                     
CRYST1   51.920   66.372  110.910  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      0.019260  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015067  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009016        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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