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Database: PDB
Entry: 5F85
LinkDB: 5F85
Original site: 5F85 
HEADER    TRANSFERASE/HYDROLASE                   09-DEC-15   5F85              
TITLE     CRYSTAL STRUCTURE OF DROSOPHILA POGLUT1 (RUMI) COMPLEXED WITH ITS     
TITLE    2 SUBSTRATE PROTEIN (EGF REPEAT) AND UDP                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: O-GLUCOSYLTRANSFERASE RUMI;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 21-407;                                       
COMPND   5 EC: 2.4.1.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: COAGULATION FACTOR IX;                                     
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 92-130;                                       
COMPND  11 SYNONYM: CHRISTMAS FACTOR,PLASMA THROMBOPLASTIN COMPONENT,PTC;       
COMPND  12 EC: 3.4.21.22;                                                       
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 GENE: RUMI, CG31152;                                                 
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: F9;                                                            
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GLYCOSYLTRANSFERASE, PROTEIN O-GLUCOSYLTRANSFERASE, NOTCH REGULATION, 
KEYWDS   2 EGF REPEAT, TRANSFERASE-HYDROLASE COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.J.YU,H.L.LI                                                         
REVDAT   2   18-APR-18 5F85    1       JRNL   REMARK                            
REVDAT   1   20-JUL-16 5F85    0                                                
JRNL        AUTH   H.YU,H.TAKEUCHI,M.TAKEUCHI,Q.LIU,J.KANTHARIA,                
JRNL        AUTH 2 R.S.HALTIWANGER,H.LI                                         
JRNL        TITL   STRUCTURAL ANALYSIS OF NOTCH-REGULATING RUMI REVEALS BASIS   
JRNL        TITL 2 FOR PATHOGENIC MUTATIONS.                                    
JRNL        REF    NAT. CHEM. BIOL.              V.  12   735 2016              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   27428513                                                     
JRNL        DOI    10.1038/NCHEMBIO.2135                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 33563                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1773                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2318                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 132                          
REMARK   3   BIN FREE R VALUE                    : 0.3680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3323                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 125                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.59000                                              
REMARK   3    B22 (A**2) : 0.59000                                              
REMARK   3    B33 (A**2) : -0.88000                                             
REMARK   3    B12 (A**2) : 0.29000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.196         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.172         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3477 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4707 ; 1.261 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   402 ; 5.932 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   177 ;32.947 ;23.390       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   585 ;15.195 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;14.019 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   468 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2679 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 5F85 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216118.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35484                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 9.300                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.62M AMMONIUM SULFATE, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000      134.91450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       77.89292            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       15.76000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000      134.91450            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       77.89292            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       15.76000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000      134.91450            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       77.89292            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       15.76000            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000      134.91450            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       77.89292            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       15.76000            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000      134.91450            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       77.89292            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       15.76000            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000      134.91450            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       77.89292            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       15.76000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      155.78585            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       31.52000            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000      155.78585            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       31.52000            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000      155.78585            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       31.52000            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000      155.78585            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       31.52000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000      155.78585            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       31.52000            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000      155.78585            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       31.52000            
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: 3590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 S    SO4 A 507  LIES ON A SPECIAL POSITION.                          
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     ALA A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     GLU A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     ASP A    22                                                      
REMARK 465     ASP A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     LEU A    25                                                      
REMARK 465     CYS A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     ASP A    29                                                      
REMARK 465     GLN A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     CYS A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     GLN A    35                                                      
REMARK 465     SER A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     ASP A    39                                                      
REMARK 465     GLN A    40                                                      
REMARK 465     ILE A    41                                                      
REMARK 465     LYS A   407                                                      
REMARK 465     ALA A   408                                                      
REMARK 465     ARG A   409                                                      
REMARK 465     ALA A   410                                                      
REMARK 465     LEU A   411                                                      
REMARK 465     VAL A   412                                                      
REMARK 465     PRO A   413                                                      
REMARK 465     ARG A   414                                                      
REMARK 465     MET B    43                                                      
REMARK 465     ASP B    44                                                      
REMARK 465     ILE B    45                                                      
REMARK 465     VAL B    46                                                      
REMARK 465     ASP B    47                                                      
REMARK 465     HIS B    87                                                      
REMARK 465     HIS B    88                                                      
REMARK 465     HIS B    89                                                      
REMARK 465     HIS B    90                                                      
REMARK 465     HIS B    91                                                      
REMARK 465     HIS B    92                                                      
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     LYS A 334    CG   CD   CE   NZ                                   
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    ASP A  70       62.76     35.39                                   
REMARK 500    MET A 143      149.81   -172.17                                   
REMARK 500    TRP A 159     -118.87    -95.08                                   
REMARK 500    ALA A 163       59.26   -109.60                                   
REMARK 500    LYS A 262      -62.71   -128.53                                   
REMARK 500    ALA A 294     -150.46   -131.48                                   
REMARK 500    TRP A 327      -26.08     78.10                                   
REMARK 500    GLN A 392       54.54   -110.83                                   
REMARK 500    SER B  68     -132.30   -124.62                                   
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 B 115        DISTANCE =  6.20 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue UDP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5F84   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5F86   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5F87   RELATED DB: PDB                                   
DBREF  5F85 A   21   407  UNP    Q8T045   RUMI_DROME      21    407             
DBREF  5F85 B   46    84  UNP    P00740   FA9_HUMAN       92    130             
SEQADV 5F85 ALA A   13  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 ALA A   14  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 GLN A   15  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 PRO A   16  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 ALA A   17  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 GLU A   18  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 ALA A   19  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 LEU A   20  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 ALA A  408  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 ARG A  409  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 ALA A  410  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 LEU A  411  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 VAL A  412  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 PRO A  413  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 ARG A  414  UNP  Q8T045              EXPRESSION TAG                 
SEQADV 5F85 MET B   43  UNP  P00740              INITIATING METHIONINE          
SEQADV 5F85 ASP B   44  UNP  P00740              EXPRESSION TAG                 
SEQADV 5F85 ILE B   45  UNP  P00740              EXPRESSION TAG                 
SEQADV 5F85 LEU B   85  UNP  P00740              EXPRESSION TAG                 
SEQADV 5F85 GLU B   86  UNP  P00740              EXPRESSION TAG                 
SEQADV 5F85 HIS B   87  UNP  P00740              EXPRESSION TAG                 
SEQADV 5F85 HIS B   88  UNP  P00740              EXPRESSION TAG                 
SEQADV 5F85 HIS B   89  UNP  P00740              EXPRESSION TAG                 
SEQADV 5F85 HIS B   90  UNP  P00740              EXPRESSION TAG                 
SEQADV 5F85 HIS B   91  UNP  P00740              EXPRESSION TAG                 
SEQADV 5F85 HIS B   92  UNP  P00740              EXPRESSION TAG                 
SEQRES   1 A  402  ALA ALA GLN PRO ALA GLU ALA LEU GLU ASP ASP GLY LEU          
SEQRES   2 A  402  CYS SER ALA ASP GLN LYS SER CYS ALA GLN SER GLU PRO          
SEQRES   3 A  402  ASP GLN ILE ASN GLU ASP GLU PHE SER PHE LYS ILE ARG          
SEQRES   4 A  402  ARG GLN ILE GLU LYS ALA ASN ALA ASP TYR LYS PRO CYS          
SEQRES   5 A  402  SER SER ASP PRO GLN ASP SER ASP CYS SER CYS HIS ALA          
SEQRES   6 A  402  ASN VAL LEU LYS ARG ASP LEU ALA PRO TYR LYS SER THR          
SEQRES   7 A  402  GLY VAL THR ARG GLN MET ILE GLU SER SER ALA ARG TYR          
SEQRES   8 A  402  GLY THR LYS TYR LYS ILE TYR GLY HIS ARG LEU TYR ARG          
SEQRES   9 A  402  ASP ALA ASN CYS MET PHE PRO ALA ARG CYS GLU GLY ILE          
SEQRES  10 A  402  GLU HIS PHE LEU LEU PRO LEU VAL ALA THR LEU PRO ASP          
SEQRES  11 A  402  MET ASP LEU ILE ILE ASN THR ARG ASP TYR PRO GLN LEU          
SEQRES  12 A  402  ASN ALA ALA TRP GLY ASN ALA ALA GLY GLY PRO VAL PHE          
SEQRES  13 A  402  SER PHE SER LYS THR LYS GLU TYR ARG ASP ILE MET TYR          
SEQRES  14 A  402  PRO ALA TRP THR PHE TRP ALA GLY GLY PRO ALA THR LYS          
SEQRES  15 A  402  LEU HIS PRO ARG GLY ILE GLY ARG TRP ASP GLN MET ARG          
SEQRES  16 A  402  GLU LYS LEU GLU LYS ARG ALA ALA ALA ILE PRO TRP SER          
SEQRES  17 A  402  GLN LYS ARG SER LEU GLY PHE PHE ARG GLY SER ARG THR          
SEQRES  18 A  402  SER ASP GLU ARG ASP SER LEU ILE LEU LEU SER ARG ARG          
SEQRES  19 A  402  ASN PRO GLU LEU VAL GLU ALA GLN TYR THR LYS ASN GLN          
SEQRES  20 A  402  GLY TRP LYS SER PRO LYS ASP THR LEU ASP ALA PRO ALA          
SEQRES  21 A  402  ALA ASP GLU VAL SER PHE GLU ASP HIS CYS LYS TYR LYS          
SEQRES  22 A  402  TYR LEU PHE ASN PHE ARG GLY VAL ALA ALA SER PHE ARG          
SEQRES  23 A  402  LEU LYS HIS LEU PHE LEU CYS LYS SER LEU VAL PHE HIS          
SEQRES  24 A  402  VAL GLY ASP GLU TRP GLN GLU PHE PHE TYR ASP GLN LEU          
SEQRES  25 A  402  LYS PRO TRP VAL HIS TYR VAL PRO LEU LYS SER TYR PRO          
SEQRES  26 A  402  SER GLN GLN GLU TYR GLU HIS ILE LEU SER PHE PHE LYS          
SEQRES  27 A  402  LYS ASN ASP ALA LEU ALA GLN GLU ILE ALA GLN ARG GLY          
SEQRES  28 A  402  TYR ASP PHE ILE TRP GLU HIS LEU ARG MET LYS ASP ILE          
SEQRES  29 A  402  LYS CYS TYR TRP ARG LYS LEU LEU LYS ARG TYR VAL LYS          
SEQRES  30 A  402  LEU LEU GLN TYR GLU VAL LYS PRO GLU ASP GLN LEU ILE          
SEQRES  31 A  402  TYR ILE GLY PRO LYS ALA ARG ALA LEU VAL PRO ARG              
SEQRES   1 B   50  MET ASP ILE VAL ASP GLY ASP GLN CYS GLU SER ASN PRO          
SEQRES   2 B   50  CYS LEU ASN GLY GLY SER CYS LYS ASP ASP ILE ASN SER          
SEQRES   3 B   50  TYR GLU CYS TRP CYS PRO PHE GLY PHE GLU GLY LYS ASN          
SEQRES   4 B   50  CYS GLU LEU LEU GLU HIS HIS HIS HIS HIS HIS                  
HET    UDP  A 501      25                                                       
HET    GOL  A 502       6                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    SO4  A 506       5                                                       
HET    SO4  A 507       5                                                       
HETNAM     UDP URIDINE-5'-DIPHOSPHATE                                           
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  UDP    C9 H14 N2 O12 P2                                             
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  SO4    5(O4 S 2-)                                                   
FORMUL  10  HOH   *125(H2 O)                                                    
HELIX    1 AA1 ASN A   42  TYR A   61  1                                  20    
HELIX    2 AA2 HIS A   76  ALA A   85  1                                  10    
HELIX    3 AA3 PRO A   86  LYS A   88  5                                   3    
HELIX    4 AA4 THR A   93  ALA A  101  1                                   9    
HELIX    5 AA5 ARG A  102  GLY A  104  5                                   3    
HELIX    6 AA6 PHE A  122  LEU A  134  1                                  13    
HELIX    7 AA7 PRO A  135  LEU A  140  5                                   6    
HELIX    8 AA8 ALA A  183  TRP A  187  5                                   5    
HELIX    9 AA9 ARG A  202  ILE A  217  1                                  16    
HELIX   10 AB1 PRO A  218  LYS A  222  5                                   5    
HELIX   11 AB2 SER A  234  GLU A  236  5                                   3    
HELIX   12 AB3 ARG A  237  ASN A  247  1                                  11    
HELIX   13 AB4 SER A  263  LEU A  268  5                                   6    
HELIX   14 AB5 SER A  277  CYS A  282  1                                   6    
HELIX   15 AB6 PHE A  297  LEU A  304  1                                   8    
HELIX   16 AB7 SER A  338  LYS A  351  1                                  14    
HELIX   17 AB8 ASN A  352  LEU A  371  1                                  20    
HELIX   18 AB9 ARG A  372  LYS A  389  1                                  18    
HELIX   19 AC1 ASP B   49  ASN B   54  5                                   6    
SHEET    1 AA1 4 MET A 143  ILE A 147  0                                        
SHEET    2 AA1 4 THR A 105  ILE A 109 -1  N  TYR A 107   O  LEU A 145           
SHEET    3 AA1 4 LEU A 114  ARG A 116 -1  O  TYR A 115   N  LYS A 108           
SHEET    4 AA1 4 ILE A 402  GLY A 405 -1  O  ILE A 404   N  LEU A 114           
SHEET    1 AA2 2 PHE A 168  SER A 169  0                                        
SHEET    2 AA2 2 ILE A 179  MET A 180  1  O  ILE A 179   N  SER A 169           
SHEET    1 AA3 5 VAL A 251  THR A 256  0                                        
SHEET    2 AA3 5 ARG A 223  SER A 231  1  N  GLY A 226   O  GLU A 252           
SHEET    3 AA3 5 TYR A 284  PHE A 290  1  O  LYS A 285   N  ARG A 223           
SHEET    4 AA3 5 LEU A 308  VAL A 312  1  O  LEU A 308   N  LYS A 285           
SHEET    5 AA3 5 VAL A 331  LEU A 333  1  O  VAL A 331   N  VAL A 309           
SHEET    1 AA4 2 SER B  61  ASP B  64  0                                        
SHEET    2 AA4 2 TYR B  69  TRP B  72 -1  O  TRP B  72   N  SER B  61           
SHEET    1 AA5 2 PHE B  77  GLU B  78  0                                        
SHEET    2 AA5 2 LEU B  84  LEU B  85 -1  O  LEU B  84   N  GLU B  78           
SSBOND   1 CYS A   64    CYS A   75                          1555   1555  2.06  
SSBOND   2 CYS A   73    CYS A  378                          1555   1555  2.03  
SSBOND   3 CYS A  120    CYS A  126                          1555   1555  2.03  
SSBOND   4 CYS A  282    CYS A  305                          1555   1555  2.08  
SSBOND   5 CYS B   51    CYS B   62                          1555   1555  2.07  
SSBOND   6 CYS B   56    CYS B   71                          1555   1555  2.03  
SSBOND   7 CYS B   73    CYS B   82                          1555   1555  2.06  
CISPEP   1 GLY A  160    ASN A  161          0        -2.24                     
CISPEP   2 GLY A  165    PRO A  166          0        -1.99                     
CISPEP   3 GLY A  405    PRO A  406          0        -2.54                     
SITE     1 AC1 18 ILE A 200  ARG A 229  GLY A 230  SER A 231                    
SITE     2 AC1 18 THR A 233  ARG A 237  GLU A 275  VAL A 276                    
SITE     3 AC1 18 PHE A 278  GLY A 292  SER A 296  ARG A 298                    
SITE     4 AC1 18 GOL A 502  HOH A 603  HOH A 611  HOH A 667                    
SITE     5 AC1 18 HOH A 670  HOH B 104                                          
SITE     1 AC2  9 ARG A 125  ASP A 151  PRO A 191  ALA A 295                    
SITE     2 AC2  9 SER A 296  PHE A 297  UDP A 501  HOH A 610                    
SITE     3 AC2  9 SER B  53                                                     
SITE     1 AC3  7 HIS A 196  MET A 206  LYS A 209  SER A 277                    
SITE     2 AC3  7 PHE A 278  GLU A 279  HOH A 667                               
SITE     1 AC4  2 ARG A 229  VAL A 276                                          
SITE     1 AC5  4 ARG A 372  MET A 373  LYS A 374  HOH A 673                    
SITE     1 AC6  6 LYS A  49  GLY A 313  ASP A 314  LYS A 334                    
SITE     2 AC6  6 SER A 335  HOH A 651                                          
SITE     1 AC7  4 SER A 239  SER A 338  GLN A 339  HOH A 614                    
CRYST1  269.829  269.829   47.280  90.00  90.00 120.00 H 3 2        18          
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      0.003706  0.002140  0.000000        0.00000                         
SCALE2      0.000000  0.004279  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021151        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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