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Database: PDB
Entry: 3A1J
LinkDB: 3A1J
Original site: 3A1J 
HEADER    HYDROLASE/CELL CYCLE                    08-APR-09   3A1J              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN RAD9-HUS1-RAD1 COMPLEX                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL CYCLE CHECKPOINT CONTROL PROTEIN RAD9A;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-266;                         
COMPND   5 SYNONYM: HRAD9, DNA REPAIR EXONUCLEASE RAD9 HOMOLOG A;               
COMPND   6 EC: 3.1.11.2;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CHECKPOINT PROTEIN HUS1;                                   
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: HHUS1;                                                      
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: CELL CYCLE CHECKPOINT PROTEIN RAD1;                        
COMPND  15 CHAIN: C;                                                            
COMPND  16 FRAGMENT: RESIDUES 13-275;                                           
COMPND  17 SYNONYM: HRAD1, DNA REPAIR EXONUCLEASE RAD1 HOMOLOG, RAD1-LIKE DNA   
COMPND  18 DAMAGE CHECKPOINT PROTEIN;                                           
COMPND  19 EC: 3.1.11.2;                                                        
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: HELA CELLS;                                               
SOURCE   6 GENE: RAD9(1-272);                                                   
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PCDF;                                     
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 CELL_LINE: HELA CELLS;                                               
SOURCE  17 GENE: HUS1;                                                          
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  25 ORGANISM_COMMON: HUMAN;                                              
SOURCE  26 ORGANISM_TAXID: 9606;                                                
SOURCE  27 CELL_LINE: HELA CELLS;                                               
SOURCE  28 GENE: RAD1;                                                          
SOURCE  29 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  30 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  31 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE  32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  33 EXPRESSION_SYSTEM_PLASMID: PCOLA                                     
KEYWDS    DNA DAMAGE, CHECKPOINT, DNA REPAIR, EXONUCLEASE, HYDROLASE, NUCLEASE, 
KEYWDS   2 NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, CYTOPLASM, ALTERNATIVE        
KEYWDS   3 SPLICING, HYDROLASE-CELL CYCLE COMPLEX                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.Y.SOHN,Y.CHO                                                        
REVDAT   4   29-JUL-20 3A1J    1       COMPND REMARK SEQADV HET                 
REVDAT   4 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   4 3                   1       ATOM                                     
REVDAT   3   30-JUN-09 3A1J    1       JRNL                                     
REVDAT   2   09-JUN-09 3A1J    1       JRNL                                     
REVDAT   1   02-JUN-09 3A1J    0                                                
JRNL        AUTH   S.Y.SOHN,Y.CHO                                               
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN RAD9-HUS1-RAD1 CLAMP          
JRNL        REF    J.MOL.BIOL.                   V. 390   490 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19464297                                                     
JRNL        DOI    10.1016/J.JMB.2009.05.028                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 116907.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 30943                          
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 SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1537                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4526                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE                    : 0.3750                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 251                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.024                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6258                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 186                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.42000                                             
REMARK   3    B22 (A**2) : 2.38000                                              
REMARK   3    B33 (A**2) : -0.95000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.54000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.32                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.43                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.700                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.630 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.840 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.450 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.660 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 38.39                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : SUC_PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  3   : SUC_TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3A1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-APR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000028694.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31999                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.27800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 0.18M KCL, 0.16M           
REMARK 280  GUANIDINE HYDROCHLORIDE, 0.33M ZWITTERGENT 3-08, PH 6.8, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 296K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.38800            
REMARK 290   SMTRY3   2  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     GLU A   185                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     ASN B    49                                                      
REMARK 465     ALA B   214                                                      
REMARK 465     SER B   215                                                      
REMARK 465     GLU B   216                                                      
REMARK 465     SER B   217                                                      
REMARK 465     THR B   218                                                      
REMARK 465     HIS B   219                                                      
REMARK 465     GLU B   220                                                      
REMARK 465     ASP B   221                                                      
REMARK 465     ARG B   222                                                      
REMARK 465     ASN B   223                                                      
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    ALA A  54      151.86    -49.29                                   
REMARK 500    GLN A  68      108.66    -55.43                                   
REMARK 500    LEU A  70       57.69   -170.88                                   
REMARK 500    LEU A  71      122.04    -28.30                                   
REMARK 500    LEU A  90      -74.29    -72.82                                   
REMARK 500    LYS A  92      -81.03    -88.50                                   
REMARK 500    PHE A 136      143.36   -171.50                                   
REMARK 500    GLU A 183     -143.67   -106.10                                   
REMARK 500    ASP A 187       39.76    -75.63                                   
REMARK 500    THR A 189     -167.67    -76.40                                   
REMARK 500    ASP A 241     -105.13   -120.37                                   
REMARK 500    GLN B  60      -45.11    -28.09                                   
REMARK 500    PHE B  63      -53.64   -127.98                                   
REMARK 500    ASN B 107       49.93   -152.36                                   
REMARK 500    LYS B 108      -78.17    -63.74                                   
REMARK 500    PHE B 110      163.06    177.96                                   
REMARK 500    SER B 123     -169.92   -106.83                                   
REMARK 500    LEU B 146       36.43   -141.28                                   
REMARK 500    VAL B 230      130.58   -170.75                                   
REMARK 500    ASN B 257      121.30    -32.84                                   
REMARK 500    ASN B 258       11.46     57.05                                   
REMARK 500    MSE B 260      154.93    178.42                                   
REMARK 500    GLU B 268       65.26     62.03                                   
REMARK 500    ASP B 269       11.35     51.04                                   
REMARK 500    LEU C  27      -55.05   -128.03                                   
REMARK 500    ASN C  55       78.85   -118.25                                   
REMARK 500    ALA C  56       64.25     39.54                                   
REMARK 500    LYS C  57       -0.78     68.22                                   
REMARK 500    LEU C 143      156.10    -47.11                                   
REMARK 500    SER C 149       -5.60    -58.76                                   
REMARK 500    ASP C 171       96.34    -52.80                                   
REMARK 500    ALA C 196       48.00     38.76                                   
REMARK 500    GLN C 217      156.30    177.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3A1J A    1   266  UNP    Q99638   RAD9A_HUMAN      1    266             
DBREF  3A1J B    1   280  UNP    O60921   HUS1_HUMAN       1    280             
DBREF  3A1J C   13   275  UNP    O60671   RAD1_HUMAN      13    275             
SEQADV 3A1J HIS B    0  UNP  O60921              EXPRESSION TAG                 
SEQRES   1 A  266  MSE LYS CYS LEU VAL THR GLY GLY ASN VAL LYS VAL LEU          
SEQRES   2 A  266  GLY LYS ALA VAL HIS SER LEU SER ARG ILE GLY ASP GLU          
SEQRES   3 A  266  LEU TYR LEU GLU PRO LEU GLU ASP GLY LEU SER LEU ARG          
SEQRES   4 A  266  THR VAL ASN SER SER ARG SER ALA TYR ALA CYS PHE LEU          
SEQRES   5 A  266  PHE ALA PRO LEU PHE PHE GLN GLN TYR GLN ALA ALA THR          
SEQRES   6 A  266  PRO GLY GLN ASP LEU LEU ARG CYS LYS ILE LEU MSE LYS          
SEQRES   7 A  266  SER PHE LEU SER VAL PHE ARG SER LEU ALA MSE LEU GLU          
SEQRES   8 A  266  LYS THR VAL GLU LYS CYS CYS ILE SER LEU ASN GLY ARG          
SEQRES   9 A  266  SER SER ARG LEU VAL VAL GLN LEU HIS CYS LYS PHE GLY          
SEQRES  10 A  266  VAL ARG LYS THR HIS ASN LEU SER PHE GLN ASP CYS GLU          
SEQRES  11 A  266  SER LEU GLN ALA VAL PHE ASP PRO ALA SER CYS PRO HIS          
SEQRES  12 A  266  MSE LEU ARG ALA PRO ALA ARG VAL LEU GLY GLU ALA VAL          
SEQRES  13 A  266  LEU PRO PHE SER PRO ALA LEU ALA GLU VAL THR LEU GLY          
SEQRES  14 A  266  ILE GLY ARG GLY ARG ARG VAL ILE LEU ARG SER TYR HIS          
SEQRES  15 A  266  GLU GLU GLU ALA ASP SER THR ALA LYS ALA MSE VAL THR          
SEQRES  16 A  266  GLU MSE CYS LEU GLY GLU GLU ASP PHE GLN GLN LEU GLN          
SEQRES  17 A  266  ALA GLN GLU GLY VAL ALA ILE THR PHE CYS LEU LYS GLU          
SEQRES  18 A  266  PHE ARG GLY LEU LEU SER PHE ALA GLU SER ALA ASN LEU          
SEQRES  19 A  266  ASN LEU SER ILE HIS PHE ASP ALA PRO GLY ARG PRO ALA          
SEQRES  20 A  266  ILE PHE THR ILE LYS ASP SER LEU LEU ASP GLY HIS PHE          
SEQRES  21 A  266  VAL LEU ALA THR LEU SER                                      
SEQRES   1 B  281  HIS MSE LYS PHE ARG ALA LYS ILE VAL ASP GLY ALA CYS          
SEQRES   2 B  281  LEU ASN HIS PHE THR ARG ILE SER ASN MSE ILE ALA LYS          
SEQRES   3 B  281  LEU ALA LYS THR CYS THR LEU ARG ILE SER PRO ASP LYS          
SEQRES   4 B  281  LEU ASN PHE ILE LEU CYS ASP LYS LEU ALA ASN GLY GLY          
SEQRES   5 B  281  VAL SER MSE TRP CYS GLU LEU GLU GLN GLU ASN PHE PHE          
SEQRES   6 B  281  ASN GLU PHE GLN MSE GLU GLY VAL SER ALA GLU ASN ASN          
SEQRES   7 B  281  GLU ILE TYR LEU GLU LEU THR SER GLU ASN LEU SER ARG          
SEQRES   8 B  281  ALA LEU LYS THR ALA GLN ASN ALA ARG ALA LEU LYS ILE          
SEQRES   9 B  281  LYS LEU THR ASN LYS HIS PHE PRO CYS LEU THR VAL SER          
SEQRES  10 B  281  VAL GLU LEU LEU SER MSE SER SER SER SER ARG ILE VAL          
SEQRES  11 B  281  THR HIS ASP ILE PRO ILE LYS VAL ILE PRO ARG LYS LEU          
SEQRES  12 B  281  TRP LYS ASP LEU GLN GLU PRO VAL VAL PRO ASP PRO ASP          
SEQRES  13 B  281  VAL SER ILE TYR LEU PRO VAL LEU LYS THR MSE LYS SER          
SEQRES  14 B  281  VAL VAL GLU LYS MSE LYS ASN ILE SER ASN HIS LEU VAL          
SEQRES  15 B  281  ILE GLU ALA ASN LEU ASP GLY GLU LEU ASN LEU LYS ILE          
SEQRES  16 B  281  GLU THR GLU LEU VAL CYS VAL THR THR HIS PHE LYS ASP          
SEQRES  17 B  281  LEU GLY ASN PRO PRO LEU ALA SER GLU SER THR HIS GLU          
SEQRES  18 B  281  ASP ARG ASN VAL GLU HIS MSE ALA GLU VAL HIS ILE ASP          
SEQRES  19 B  281  ILE ARG LYS LEU LEU GLN PHE LEU ALA GLY GLN GLN VAL          
SEQRES  20 B  281  ASN PRO THR LYS ALA LEU CYS ASN ILE VAL ASN ASN LYS          
SEQRES  21 B  281  MSE VAL HIS PHE ASP LEU LEU HIS GLU ASP VAL SER LEU          
SEQRES  22 B  281  GLN TYR PHE ILE PRO ALA LEU SER                              
SEQRES   1 C  263  ASP GLN TYR SER LEU VAL ALA SER LEU ASP ASN VAL ARG          
SEQRES   2 C  263  ASN LEU SER THR ILE LEU LYS ALA ILE HIS PHE ARG GLU          
SEQRES   3 C  263  HIS ALA THR CYS PHE ALA THR LYS ASN GLY ILE LYS VAL          
SEQRES   4 C  263  THR VAL GLU ASN ALA LYS CYS VAL GLN ALA ASN ALA PHE          
SEQRES   5 C  263  ILE GLN ALA GLY ILE PHE GLN GLU PHE LYS VAL GLN GLU          
SEQRES   6 C  263  GLU SER VAL THR PHE ARG ILE ASN LEU THR VAL LEU LEU          
SEQRES   7 C  263  ASP CYS LEU SER ILE PHE GLY SER SER PRO MSE PRO GLY          
SEQRES   8 C  263  THR LEU THR ALA LEU ARG MSE CYS TYR GLN GLY TYR GLY          
SEQRES   9 C  263  TYR PRO LEU MSE LEU PHE LEU GLU GLU GLY GLY VAL VAL          
SEQRES  10 C  263  THR VAL CYS LYS ILE ASN THR GLN GLU PRO GLU GLU THR          
SEQRES  11 C  263  LEU ASP PHE ASP PHE CYS SER THR ASN VAL ILE ASN LYS          
SEQRES  12 C  263  ILE ILE LEU GLN SER GLU GLY LEU ARG GLU ALA PHE SER          
SEQRES  13 C  263  GLU LEU ASP MSE THR SER GLU VAL LEU GLN ILE THR MSE          
SEQRES  14 C  263  SER PRO ASP LYS PRO TYR PHE ARG LEU SER THR PHE GLY          
SEQRES  15 C  263  ASN ALA GLY SER SER HIS LEU ASP TYR PRO LYS ASP SER          
SEQRES  16 C  263  ASP LEU MSE GLU ALA PHE HIS CYS ASN GLN THR GLN VAL          
SEQRES  17 C  263  ASN ARG TYR LYS ILE SER LEU LEU LYS PRO SER THR LYS          
SEQRES  18 C  263  ALA LEU VAL LEU SER CYS LYS VAL SER ILE ARG THR ASP          
SEQRES  19 C  263  ASN ARG GLY PHE LEU SER LEU GLN TYR MSE ILE ARG ASN          
SEQRES  20 C  263  GLU ASP GLY GLN ILE CYS PHE VAL GLU TYR TYR CYS CYS          
SEQRES  21 C  263  PRO ASP GLU                                                  
MODRES 3A1J MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE A   77  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE A   89  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE A  144  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE A  193  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE A  197  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE B   22  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE B   54  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE B   69  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE B  122  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE B  166  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE B  173  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE B  227  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE B  260  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE C  101  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE C  110  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE C  120  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE C  172  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE C  181  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE C  210  MET  SELENOMETHIONINE                                   
MODRES 3A1J MSE C  256  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  77       8                                                       
HET    MSE  A  89       8                                                       
HET    MSE  A 144       8                                                       
HET    MSE  A 193       8                                                       
HET    MSE  A 197       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  22       8                                                       
HET    MSE  B  54       8                                                       
HET    MSE  B  69       8                                                       
HET    MSE  B 122       8                                                       
HET    MSE  B 166       8                                                       
HET    MSE  B 173       8                                                       
HET    MSE  B 227       8                                                       
HET    MSE  B 260       8                                                       
HET    MSE  C 101       8                                                       
HET    MSE  C 110       8                                                       
HET    MSE  C 120       8                                                       
HET    MSE  C 172       8                                                       
HET    MSE  C 181       8                                                       
HET    MSE  C 210       8                                                       
HET    MSE  C 256       8                                                       
HET    GLC  D   1      11                                                       
HET    FRU  D   2      12                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     FRU BETA-D-FRUCTOFURANOSE                                            
FORMUL   1  MSE    22(C5 H11 N O2 SE)                                           
FORMUL   4  GLC    C6 H12 O6                                                    
FORMUL   4  FRU    C6 H12 O6                                                    
FORMUL   5  HOH   *186(H2 O)                                                    
HELIX    1   1 GLY A    7  ARG A   22  1                                  16    
HELIX    2   2 PRO A   55  PHE A   58  5                                   4    
HELIX    3   3 MSE A   77  ARG A   85  1                                   9    
HELIX    4   4 SER A   86  THR A   93  1                                   8    
HELIX    5   5 ASP A  137  CYS A  141  5                                   5    
HELIX    6   6 ALA A  149  LEU A  157  1                                   9    
HELIX    7   7 ARG A  172  ARG A  174  5                                   3    
HELIX    8   8 GLY A  200  PHE A  204  5                                   5    
HELIX    9   9 LEU A  219  ALA A  232  1                                  14    
HELIX   10  10 ASP B    9  ALA B   27  1                                  19    
HELIX   11  11 GLU B   61  PHE B   63  5                                   3    
HELIX   12  12 SER B   85  LEU B   92  1                                   8    
HELIX   13  13 LYS B   93  GLN B   96  5                                   4    
HELIX   14  14 PRO B  139  GLN B  147  5                                   9    
HELIX   15  15 VAL B  162  ASN B  175  1                                  14    
HELIX   16  16 ILE B  234  GLN B  244  1                                  11    
HELIX   17  17 VAL C   24  ALA C   33  1                                  10    
HELIX   18  18 GLY C   68  PHE C   70  5                                   3    
HELIX   19  19 LEU C   86  SER C   94  1                                   9    
HELIX   20  20 LEU C  163  GLU C  169  1                                   7    
HELIX   21  21 ILE C  225  LYS C  229  1                                   5    
HELIX   22  22 PRO C  230  SER C  238  1                                   9    
SHEET    1   A 9 GLN A  60  GLN A  62  0                                        
SHEET    2   A 9 LYS A   2  THR A   6 -1  N  LEU A   4   O  GLN A  60           
SHEET    3   A 9 VAL A  94  SER A 100 -1  O  CYS A  97   N  VAL A   5           
SHEET    4   A 9 ARG A 107  CYS A 114 -1  O  HIS A 113   N  LYS A  96           
SHEET    5   A 9 ARG A 119  SER A 125 -1  O  LEU A 124   N  LEU A 108           
SHEET    6   A 9 GLY C 197  TYR C 203 -1  O  SER C 198   N  ASN A 123           
SHEET    7   A 9 PHE C 188  GLY C 194 -1  N  GLY C 194   O  GLY C 197           
SHEET    8   A 9 VAL C 176  MSE C 181 -1  N  GLN C 178   O  SER C 191           
SHEET    9   A 9 GLN C 219  LYS C 224 -1  O  ASN C 221   N  ILE C 179           
SHEET    1   B10 GLN A 127  ASP A 128  0                                        
SHEET    2   B10 CYS A  73  LEU A  76 -1  N  LYS A  74   O  GLN A 127           
SHEET    3   B10 GLU A  26  LEU A  32 -1  N  LEU A  27   O  ILE A  75           
SHEET    4   B10 GLY A  35  VAL A  41 -1  O  ARG A  39   N  TYR A  28           
SHEET    5   B10 ALA A  47  PHE A  53 -1  O  PHE A  53   N  LEU A  36           
SHEET    6   B10 LEU A 256  LEU A 262 -1  O  VAL A 261   N  TYR A  48           
SHEET    7   B10 ALA A 247  LYS A 252 -1  N  ALA A 247   O  LEU A 262           
SHEET    8   B10 ASN A 235  PHE A 240 -1  N  HIS A 239   O  ILE A 248           
SHEET    9   B10 HIS A 143  PRO A 148 -1  N  ALA A 147   O  LEU A 236           
SHEET   10   B10 GLN A 206  GLN A 208 -1  O  GLN A 208   N  MSE A 144           
SHEET    1   C 9 ALA A 214  CYS A 218  0                                        
SHEET    2   C 9 GLU A 165  ILE A 170 -1  N  LEU A 168   O  ILE A 215           
SHEET    3   C 9 VAL A 176  TYR A 181 -1  O  ARG A 179   N  THR A 167           
SHEET    4   C 9 VAL A 194  LEU A 199 -1  O  MSE A 197   N  LEU A 178           
SHEET    5   C 9 ILE B 128  PRO B 134 -1  O  THR B 130   N  GLU A 196           
SHEET    6   C 9 CYS B 112  LEU B 119 -1  N  VAL B 117   O  VAL B 129           
SHEET    7   C 9 ALA B  98  THR B 106 -1  N  ARG B  99   O  GLU B 118           
SHEET    8   C 9 LYS B   2  ILE B   7 -1  N  ALA B   5   O  ILE B 103           
SHEET    9   C 9 GLU B  66  GLU B  70 -1  O  GLN B  68   N  ARG B   4           
SHEET    1   D 9 LYS B 136  VAL B 137  0                                        
SHEET    2   D 9 ILE B  79  THR B  84 -1  N  GLU B  82   O  LYS B 136           
SHEET    3   D 9 THR B  29  ILE B  34 -1  N  LEU B  32   O  LEU B  81           
SHEET    4   D 9 LYS B  38  LEU B  43 -1  O  ILE B  42   N  THR B  31           
SHEET    5   D 9 SER B  53  GLU B  59 -1  O  LEU B  58   N  LEU B  39           
SHEET    6   D 9 SER B 271  PRO B 277 -1  O  GLN B 273   N  TRP B  55           
SHEET    7   D 9 MSE B 260  LEU B 266 -1  N  VAL B 261   O  ILE B 276           
SHEET    8   D 9 LYS B 250  VAL B 256 -1  N  VAL B 256   O  MSE B 260           
SHEET    9   D 9 VAL B 156  TYR B 159 -1  N  ILE B 158   O  CYS B 253           
SHEET    1   E 9 ALA B 228  ASP B 233  0                                        
SHEET    2   E 9 HIS B 179  ALA B 184 -1  N  LEU B 180   O  ILE B 232           
SHEET    3   E 9 LEU B 190  GLU B 195 -1  O  ASN B 191   N  GLU B 183           
SHEET    4   E 9 VAL B 199  PHE B 205 -1  O  PHE B 205   N  LEU B 190           
SHEET    5   E 9 VAL C 128  ILE C 134 -1  O  VAL C 129   N  HIS B 204           
SHEET    6   E 9 LEU C 119  GLU C 125 -1  N  LEU C 119   O  ILE C 134           
SHEET    7   E 9 ALA C 107  TYR C 112 -1  N  CYS C 111   O  MSE C 120           
SHEET    8   E 9 LEU C  17  LEU C  21 -1  N  ALA C  19   O  MSE C 110           
SHEET    9   E 9 GLU C  72  VAL C  75 -1  O  LYS C  74   N  VAL C  18           
SHEET    1   F 9 VAL C  80  ASN C  85  0                                        
SHEET    2   F 9 HIS C  39  THR C  45 -1  N  CYS C  42   O  PHE C  82           
SHEET    3   F 9 GLY C  48  ASN C  55 -1  O  THR C  52   N  THR C  41           
SHEET    4   F 9 VAL C  59  GLN C  66 -1  O  VAL C  59   N  ASN C  55           
SHEET    5   F 9 ILE C 264  CYS C 271 -1  O  GLU C 268   N  ASN C  62           
SHEET    6   F 9 LEU C 251  ARG C 258 -1  N  ILE C 257   O  CYS C 265           
SHEET    7   F 9 LYS C 240  ASP C 246 -1  N  ARG C 244   O  SER C 252           
SHEET    8   F 9 VAL C 152  GLN C 159 -1  N  ILE C 156   O  ILE C 243           
SHEET    9   F 9 MSE C 210  CYS C 215 -1  O  HIS C 214   N  LYS C 155           
LINK         C   MSE A   1                 N   LYS A   2     1555   1555  1.32  
LINK         C   LEU A  76                 N   MSE A  77     1555   1555  1.33  
LINK         C   MSE A  77                 N   LYS A  78     1555   1555  1.33  
LINK         C   ALA A  88                 N   MSE A  89     1555   1555  1.33  
LINK         C   MSE A  89                 N   LEU A  90     1555   1555  1.33  
LINK         C   HIS A 143                 N   MSE A 144     1555   1555  1.32  
LINK         C   MSE A 144                 N   LEU A 145     1555   1555  1.33  
LINK         C   ALA A 192                 N   MSE A 193     1555   1555  1.33  
LINK         C   MSE A 193                 N   VAL A 194     1555   1555  1.33  
LINK         C   GLU A 196                 N   MSE A 197     1555   1555  1.33  
LINK         C   MSE A 197                 N   CYS A 198     1555   1555  1.33  
LINK         C   HIS B   0                 N   MSE B   1     1555   1555  1.33  
LINK         C   MSE B   1                 N   LYS B   2     1555   1555  1.32  
LINK         C   ASN B  21                 N   MSE B  22     1555   1555  1.33  
LINK         C   MSE B  22                 N   ILE B  23     1555   1555  1.33  
LINK         C   SER B  53                 N   MSE B  54     1555   1555  1.33  
LINK         C   MSE B  54                 N   TRP B  55     1555   1555  1.33  
LINK         C   GLN B  68                 N   MSE B  69     1555   1555  1.33  
LINK         C   MSE B  69                 N   GLU B  70     1555   1555  1.32  
LINK         C   SER B 121                 N   MSE B 122     1555   1555  1.33  
LINK         C   MSE B 122                 N   SER B 123     1555   1555  1.33  
LINK         C   THR B 165                 N   MSE B 166     1555   1555  1.33  
LINK         C   MSE B 166                 N   LYS B 167     1555   1555  1.33  
LINK         C   LYS B 172                 N   MSE B 173     1555   1555  1.33  
LINK         C   MSE B 173                 N   LYS B 174     1555   1555  1.33  
LINK         C   HIS B 226                 N   MSE B 227     1555   1555  1.32  
LINK         C   MSE B 227                 N   ALA B 228     1555   1555  1.33  
LINK         C   LYS B 259                 N   MSE B 260     1555   1555  1.33  
LINK         C   MSE B 260                 N   VAL B 261     1555   1555  1.33  
LINK         C   PRO C 100                 N   MSE C 101     1555   1555  1.33  
LINK         C   MSE C 101                 N   PRO C 102     1555   1555  1.35  
LINK         C   ARG C 109                 N   MSE C 110     1555   1555  1.33  
LINK         C   MSE C 110                 N   CYS C 111     1555   1555  1.33  
LINK         C   LEU C 119                 N   MSE C 120     1555   1555  1.33  
LINK         C   MSE C 120                 N   LEU C 121     1555   1555  1.33  
LINK         C   ASP C 171                 N   MSE C 172     1555   1555  1.33  
LINK         C   MSE C 172                 N   THR C 173     1555   1555  1.33  
LINK         C   THR C 180                 N   MSE C 181     1555   1555  1.32  
LINK         C   MSE C 181                 N   SER C 182     1555   1555  1.33  
LINK         C   LEU C 209                 N   MSE C 210     1555   1555  1.33  
LINK         C   MSE C 210                 N   GLU C 211     1555   1555  1.33  
LINK         C   TYR C 255                 N   MSE C 256     1555   1555  1.33  
LINK         C   MSE C 256                 N   ILE C 257     1555   1555  1.33  
LINK         C1  GLC D   1                 O2  FRU D   2     1555   1555  1.46  
CISPEP   1 LYS C  185    PRO C  186          0        -0.20                     
CRYST1   77.154   70.776   86.661  90.00  99.20  90.00 P 1 21 1      2          
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      0.012961  0.000000  0.002099        0.00000                         
SCALE2      0.000000  0.014129  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011690        0.00000                         
HETATM    1  N   MSE A   1      40.026  37.636  32.315  1.00 49.49           N  
HETATM    2  CA  MSE A   1      38.863  37.565  33.228  1.00 47.97           C  
HETATM    3  C   MSE A   1      37.591  37.797  32.444  1.00 45.56           C  
HETATM    4  O   MSE A   1      37.541  38.663  31.587  1.00 44.80           O  
HETATM    5  CB  MSE A   1      38.968  38.637  34.304  1.00 51.87           C  
HETATM    6  CG  MSE A   1      37.719  38.720  35.159  1.00 57.88           C  
HETATM    7 SE   MSE A   1      37.226  40.532  35.618  1.00 67.03          SE  
HETATM    8  CE  MSE A   1      36.671  41.119  33.857  1.00 61.70           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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