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Database: PDB
Entry: 3A98
LinkDB: 3A98
Original site: 3A98 
HEADER    SIGNALING PROTEIN                       21-OCT-09   3A98              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF THE INTERACTING REGIONS OF DOCK2  
TITLE    2 AND ELMO1                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DEDICATOR OF CYTOKINESIS PROTEIN 2;                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: N-TERMINAL DOMAINS, SH3 DOMAIN, RESIDUES 1-177;            
COMPND   5 SYNONYM: DOCK2;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ENGULFMENT AND CELL MOTILITY PROTEIN 1;                    
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: C-TERMINAL DOMAINS, PH DOMAIN, RESIDUES 532-727;           
COMPND  11 SYNONYM: ELMO1, CED-12 HOMOLOG;                                      
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DOCK2, KIAA0209;                                               
SOURCE   6 EXPRESSION_SYSTEM: CELL FREE PROTEIN SYNTHESIS;                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PX080711-01;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: ELMO1, KIAA0281;                                               
SOURCE  14 EXPRESSION_SYSTEM: CELL FREE PROTEIN SYNTHESIS;                      
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PX080910-01                               
KEYWDS    PROTEIN-PROTEIN COMPLEX, DOCK2, ELMO1, SH3 DOMAIN, PH DOMAIN, HELIX   
KEYWDS   2 BUNDLE, PROLINE-RICH SEQUENCE, CYTOSKELETON, GUANINE-NUCLEOTIDE      
KEYWDS   3 RELEASING FACTOR, MEMBRANE, PHOSPHOPROTEIN, APOPTOSIS, CELL          
KEYWDS   4 MEMBRANE, PHAGOCYTOSIS, SH3-BINDING, SIGNALING PROTEIN               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.HANAWA-SUETSUGU,M.KUKIMOTO-NIINO,S.SEKINE,T.ITO,C.MISHIMA-          
AUTHOR   2 TSUMAGARI,T.TERADA,M.SHIROUZU,Y.FUKUI,S.YOKOYAMA                     
REVDAT   2   04-SEP-19 3A98    1       JRNL   LINK                              
REVDAT   1   27-OCT-10 3A98    0                                                
JRNL        AUTH   K.HANAWA-SUETSUGU,M.KUKIMOTO-NIINO,C.MISHIMA-TSUMAGARI,      
JRNL        AUTH 2 R.AKASAKA,N.OHSAWA,S.SEKINE,T.ITO,N.TOCHIO,S.KOSHIBA,        
JRNL        AUTH 3 T.KIGAWA,T.TERADA,M.SHIROUZU,A.NISHIKIMI,T.URUNO,T.KATAKAI,  
JRNL        AUTH 4 T.KINASHI,D.KOHDA,Y.FUKUI,S.YOKOYAMA                         
JRNL        TITL   STRUCTURAL BASIS FOR MUTUAL RELIEF OF THE RAC GUANINE        
JRNL        TITL 2 NUCLEOTIDE EXCHANGE FACTOR DOCK2 AND ITS PARTNER ELMO1 FROM  
JRNL        TITL 3 THEIR AUTOINHIBITED FORMS.                                   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109  3305 2012              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   22331897                                                     
JRNL        DOI    10.1073/PNAS.1113512109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1994021.880                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 48976                          
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) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2455                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7485                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560                       
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 375                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5417                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 133                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.54000                                              
REMARK   3    B22 (A**2) : -2.12000                                             
REMARK   3    B33 (A**2) : -6.42000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
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) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.800                           
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 59.66                                                
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3A98 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-OCT-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000028970.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97888                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49140                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
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) : 0.78500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 3350, 0.1M DI-AMMONIUM           
REMARK 280  HYDROGEN CITRATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.91850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.36550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.01400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       62.36550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.91850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.01400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 4620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 4740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLY A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     SER A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     THR A    70                                                      
REMARK 465     VAL A    71                                                      
REMARK 465     GLU A    72                                                      
REMARK 465     LYS A    73                                                      
REMARK 465     ARG A    74                                                      
REMARK 465     ARG A    75                                                      
REMARK 465     ASN A    76                                                      
REMARK 465     THR A    77                                                      
REMARK 465     GLU A    78                                                      
REMARK 465     ASN A    79                                                      
REMARK 465     ILE A    80                                                      
REMARK 465     GLU A   168                                                      
REMARK 465     ASP A   169                                                      
REMARK 465     GLY A   170                                                      
REMARK 465     ASN A   171                                                      
REMARK 465     ILE A   172                                                      
REMARK 465     LEU A   173                                                      
REMARK 465     ASP A   174                                                      
REMARK 465     PRO A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     ASN A   177                                                      
REMARK 465     GLY B   525                                                      
REMARK 465     SER B   526                                                      
REMARK 465     SER B   527                                                      
REMARK 465     GLY B   528                                                      
REMARK 465     SER B   529                                                      
REMARK 465     LYS B   626                                                      
REMARK 465     GLU B   627                                                      
REMARK 465     LYS B   628                                                      
REMARK 465     GLY B   629                                                      
REMARK 465     ALA B   630                                                      
REMARK 465     LEU B   631                                                      
REMARK 465     LYS B   632                                                      
REMARK 465     GLN B   633                                                      
REMARK 465     GLY C    -6                                                      
REMARK 465     SER C    -5                                                      
REMARK 465     SER C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     VAL C    71                                                      
REMARK 465     GLU C    72                                                      
REMARK 465     LYS C    73                                                      
REMARK 465     ARG C    74                                                      
REMARK 465     ARG C    75                                                      
REMARK 465     ASN C    76                                                      
REMARK 465     THR C    77                                                      
REMARK 465     GLU C    78                                                      
REMARK 465     ASN C    79                                                      
REMARK 465     ILE C    80                                                      
REMARK 465     ILE C    81                                                      
REMARK 465     LEU C   163                                                      
REMARK 465     ILE C   164                                                      
REMARK 465     VAL C   165                                                      
REMARK 465     ARG C   166                                                      
REMARK 465     ASP C   167                                                      
REMARK 465     GLU C   168                                                      
REMARK 465     ASP C   169                                                      
REMARK 465     GLY C   170                                                      
REMARK 465     ASN C   171                                                      
REMARK 465     ILE C   172                                                      
REMARK 465     LEU C   173                                                      
REMARK 465     ASP C   174                                                      
REMARK 465     PRO C   175                                                      
REMARK 465     ASP C   176                                                      
REMARK 465     ASN C   177                                                      
REMARK 465     GLY D   525                                                      
REMARK 465     SER D   526                                                      
REMARK 465     SER D   527                                                      
REMARK 465     GLY D   528                                                      
REMARK 465     LEU D   565                                                      
REMARK 465     ASN D   566                                                      
REMARK 465     ALA D   567                                                      
REMARK 465     ARG D   568                                                      
REMARK 465     ARG D   569                                                      
REMARK 465     ARG D   570                                                      
REMARK 465     GLN D   571                                                      
REMARK 465     ASP D   572                                                      
REMARK 465     LYS D   573                                                      
REMARK 465     LEU D   591                                                      
REMARK 465     GLU D   592                                                      
REMARK 465     GLU D   593                                                      
REMARK 465     SER D   594                                                      
REMARK 465     PRO D   595                                                      
REMARK 465     GLN D   596                                                      
REMARK 465     GLY D   597                                                      
REMARK 465     GLU D   598                                                      
REMARK 465     VAL D   599                                                      
REMARK 465     PRO D   600                                                      
REMARK 465     HIS D   601                                                      
REMARK 465     ASP D   602                                                      
REMARK 465     SER D   603                                                      
REMARK 465     LEU D   604                                                      
REMARK 465     GLN D   605                                                      
REMARK 465     LYS D   626                                                      
REMARK 465     GLU D   627                                                      
REMARK 465     LYS D   628                                                      
REMARK 465     GLY D   629                                                      
REMARK 465     ALA D   630                                                      
REMARK 465     LEU D   631                                                      
REMARK 465     LYS D   632                                                      
REMARK 465     GLN D   633                                                      
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   8      -88.47    -75.69                                   
REMARK 500    HIS A  52       64.53   -165.30                                   
REMARK 500    ARG A 166      144.08    -29.14                                   
REMARK 500    ARG B 569       76.88     32.03                                   
REMARK 500    ARG B 570       17.44     52.76                                   
REMARK 500    GLU B 598       68.82   -164.72                                   
REMARK 500    ASP B 647     -137.97     39.95                                   
REMARK 500    SER B 648      -92.90    -60.15                                   
REMARK 500    MSE C   1       19.34   -142.33                                   
REMARK 500    LYS C   9      -88.16    -71.28                                   
REMARK 500    CYS C  41      103.78   -163.85                                   
REMARK 500    VAL C  69       15.97   -143.81                                   
REMARK 500    LEU D 608      100.84   -161.63                                   
REMARK 500    ALA D 611       -4.43    -58.15                                   
REMARK 500    PRO D 623        0.86    -58.72                                   
REMARK 500    ASP D 647     -149.16     50.90                                   
REMARK 500    SER D 648      -97.96    -61.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3A98 A    1   177  UNP    Q92608   DOCK2_HUMAN      1    177             
DBREF  3A98 B  532   727  UNP    Q92556   ELMO1_HUMAN    532    727             
DBREF  3A98 C    1   177  UNP    Q92608   DOCK2_HUMAN      1    177             
DBREF  3A98 D  532   727  UNP    Q92556   ELMO1_HUMAN    532    727             
SEQADV 3A98 GLY A   -6  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 SER A   -5  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 SER A   -4  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 GLY A   -3  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 SER A   -2  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 SER A   -1  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 GLY A    0  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 GLY B  525  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 SER B  526  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 SER B  527  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 GLY B  528  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 SER B  529  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 SER B  530  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 GLY B  531  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 GLY C   -6  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 SER C   -5  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 SER C   -4  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 GLY C   -3  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 SER C   -2  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 SER C   -1  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 GLY C    0  UNP  Q92608              EXPRESSION TAG                 
SEQADV 3A98 GLY D  525  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 SER D  526  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 SER D  527  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 GLY D  528  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 SER D  529  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 SER D  530  UNP  Q92556              EXPRESSION TAG                 
SEQADV 3A98 GLY D  531  UNP  Q92556              EXPRESSION TAG                 
SEQRES   1 A  184  GLY SER SER GLY SER SER GLY MSE ALA PRO TRP ARG LYS          
SEQRES   2 A  184  ALA ASP LYS GLU ARG HIS GLY VAL ALA ILE TYR ASN PHE          
SEQRES   3 A  184  GLN GLY SER GLY ALA PRO GLN LEU SER LEU GLN ILE GLY          
SEQRES   4 A  184  ASP VAL VAL ARG ILE GLN GLU THR CYS GLY ASP TRP TYR          
SEQRES   5 A  184  ARG GLY TYR LEU ILE LYS HIS LYS MSE LEU GLN GLY ILE          
SEQRES   6 A  184  PHE PRO LYS SER PHE ILE HIS ILE LYS GLU VAL THR VAL          
SEQRES   7 A  184  GLU LYS ARG ARG ASN THR GLU ASN ILE ILE PRO ALA GLU          
SEQRES   8 A  184  ILE PRO LEU ALA GLN GLU VAL THR THR THR LEU TRP GLU          
SEQRES   9 A  184  TRP GLY SER ILE TRP LYS GLN LEU TYR VAL ALA SER LYS          
SEQRES  10 A  184  LYS GLU ARG PHE LEU GLN VAL GLN SER MSE MSE TYR ASP          
SEQRES  11 A  184  LEU MSE GLU TRP ARG SER GLN LEU LEU SER GLY THR LEU          
SEQRES  12 A  184  PRO LYS ASP GLU LEU LYS GLU LEU LYS GLN LYS VAL THR          
SEQRES  13 A  184  SER LYS ILE ASP TYR GLY ASN LYS ILE LEU GLU LEU ASP          
SEQRES  14 A  184  LEU ILE VAL ARG ASP GLU ASP GLY ASN ILE LEU ASP PRO          
SEQRES  15 A  184  ASP ASN                                                      
SEQRES   1 B  203  GLY SER SER GLY SER SER GLY PRO ILE LEU GLU LEU LYS          
SEQRES   2 B  203  GLU LYS ILE GLN PRO GLU ILE LEU GLU LEU ILE LYS GLN          
SEQRES   3 B  203  GLN ARG LEU ASN ARG LEU VAL GLU GLY THR CYS PHE ARG          
SEQRES   4 B  203  LYS LEU ASN ALA ARG ARG ARG GLN ASP LYS PHE TRP TYR          
SEQRES   5 B  203  CYS ARG LEU SER PRO ASN HIS LYS VAL LEU HIS TYR GLY          
SEQRES   6 B  203  ASP LEU GLU GLU SER PRO GLN GLY GLU VAL PRO HIS ASP          
SEQRES   7 B  203  SER LEU GLN ASP LYS LEU PRO VAL ALA ASP ILE LYS ALA          
SEQRES   8 B  203  VAL VAL THR GLY LYS ASP CYS PRO HIS MSE LYS GLU LYS          
SEQRES   9 B  203  GLY ALA LEU LYS GLN ASN LYS GLU VAL LEU GLU LEU ALA          
SEQRES  10 B  203  PHE SER ILE LEU TYR ASP SER ASN CYS GLN LEU ASN PHE          
SEQRES  11 B  203  ILE ALA PRO ASP LYS HIS GLU TYR CYS ILE TRP THR ASP          
SEQRES  12 B  203  GLY LEU ASN ALA LEU LEU GLY LYS ASP MSE MSE SER ASP          
SEQRES  13 B  203  LEU THR ARG ASN ASP LEU ASP THR LEU LEU SER MSE GLU          
SEQRES  14 B  203  ILE LYS LEU ARG LEU LEU ASP LEU GLU ASN ILE GLN ILE          
SEQRES  15 B  203  PRO ASP ALA PRO PRO PRO ILE PRO LYS GLU PRO SER ASN          
SEQRES  16 B  203  TYR ASP PHE VAL TYR ASP CYS ASN                              
SEQRES   1 C  184  GLY SER SER GLY SER SER GLY MSE ALA PRO TRP ARG LYS          
SEQRES   2 C  184  ALA ASP LYS GLU ARG HIS GLY VAL ALA ILE TYR ASN PHE          
SEQRES   3 C  184  GLN GLY SER GLY ALA PRO GLN LEU SER LEU GLN ILE GLY          
SEQRES   4 C  184  ASP VAL VAL ARG ILE GLN GLU THR CYS GLY ASP TRP TYR          
SEQRES   5 C  184  ARG GLY TYR LEU ILE LYS HIS LYS MSE LEU GLN GLY ILE          
SEQRES   6 C  184  PHE PRO LYS SER PHE ILE HIS ILE LYS GLU VAL THR VAL          
SEQRES   7 C  184  GLU LYS ARG ARG ASN THR GLU ASN ILE ILE PRO ALA GLU          
SEQRES   8 C  184  ILE PRO LEU ALA GLN GLU VAL THR THR THR LEU TRP GLU          
SEQRES   9 C  184  TRP GLY SER ILE TRP LYS GLN LEU TYR VAL ALA SER LYS          
SEQRES  10 C  184  LYS GLU ARG PHE LEU GLN VAL GLN SER MSE MSE TYR ASP          
SEQRES  11 C  184  LEU MSE GLU TRP ARG SER GLN LEU LEU SER GLY THR LEU          
SEQRES  12 C  184  PRO LYS ASP GLU LEU LYS GLU LEU LYS GLN LYS VAL THR          
SEQRES  13 C  184  SER LYS ILE ASP TYR GLY ASN LYS ILE LEU GLU LEU ASP          
SEQRES  14 C  184  LEU ILE VAL ARG ASP GLU ASP GLY ASN ILE LEU ASP PRO          
SEQRES  15 C  184  ASP ASN                                                      
SEQRES   1 D  203  GLY SER SER GLY SER SER GLY PRO ILE LEU GLU LEU LYS          
SEQRES   2 D  203  GLU LYS ILE GLN PRO GLU ILE LEU GLU LEU ILE LYS GLN          
SEQRES   3 D  203  GLN ARG LEU ASN ARG LEU VAL GLU GLY THR CYS PHE ARG          
SEQRES   4 D  203  LYS LEU ASN ALA ARG ARG ARG GLN ASP LYS PHE TRP TYR          
SEQRES   5 D  203  CYS ARG LEU SER PRO ASN HIS LYS VAL LEU HIS TYR GLY          
SEQRES   6 D  203  ASP LEU GLU GLU SER PRO GLN GLY GLU VAL PRO HIS ASP          
SEQRES   7 D  203  SER LEU GLN ASP LYS LEU PRO VAL ALA ASP ILE LYS ALA          
SEQRES   8 D  203  VAL VAL THR GLY LYS ASP CYS PRO HIS MSE LYS GLU LYS          
SEQRES   9 D  203  GLY ALA LEU LYS GLN ASN LYS GLU VAL LEU GLU LEU ALA          
SEQRES  10 D  203  PHE SER ILE LEU TYR ASP SER ASN CYS GLN LEU ASN PHE          
SEQRES  11 D  203  ILE ALA PRO ASP LYS HIS GLU TYR CYS ILE TRP THR ASP          
SEQRES  12 D  203  GLY LEU ASN ALA LEU LEU GLY LYS ASP MSE MSE SER ASP          
SEQRES  13 D  203  LEU THR ARG ASN ASP LEU ASP THR LEU LEU SER MSE GLU          
SEQRES  14 D  203  ILE LYS LEU ARG LEU LEU ASP LEU GLU ASN ILE GLN ILE          
SEQRES  15 D  203  PRO ASP ALA PRO PRO PRO ILE PRO LYS GLU PRO SER ASN          
SEQRES  16 D  203  TYR ASP PHE VAL TYR ASP CYS ASN                              
MODRES 3A98 MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE A   54  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE A  120  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE A  121  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE A  125  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE B  625  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE B  677  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE B  678  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE B  692  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE C   54  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE C  120  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE C  121  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE C  125  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE D  625  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE D  677  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE D  678  MET  SELENOMETHIONINE                                   
MODRES 3A98 MSE D  692  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  54       8                                                       
HET    MSE  A 120       8                                                       
HET    MSE  A 121       8                                                       
HET    MSE  A 125       8                                                       
HET    MSE  B 625       8                                                       
HET    MSE  B 677       8                                                       
HET    MSE  B 678       8                                                       
HET    MSE  B 692       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C  54       8                                                       
HET    MSE  C 120       8                                                       
HET    MSE  C 121       8                                                       
HET    MSE  C 125       8                                                       
HET    MSE  D 625       8                                                       
HET    MSE  D 677       8                                                       
HET    MSE  D 678       8                                                       
HET    MSE  D 692       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    18(C5 H11 N O2 SE)                                           
FORMUL   5  HOH   *133(H2 O)                                                    
HELIX    1   1 ALA A   83  ALA A  108  1                                  26    
HELIX    2   2 LYS A  110  GLY A  134  1                                  25    
HELIX    3   3 PRO A  137  LEU A  159  1                                  23    
HELIX    4   4 SER B  530  GLY B  559  1                                  30    
HELIX    5   5 LYS B  620  CYS B  622  5                                   3    
HELIX    6   6 VAL B  637  GLU B  639  5                                   3    
HELIX    7   7 ASP B  658  LEU B  673  1                                  16    
HELIX    8   8 SER B  679  LEU B  698  1                                  20    
HELIX    9   9 LEU B  699  GLU B  702  5                                   4    
HELIX   10  10 GLU C   84  ALA C  108  1                                  25    
HELIX   11  11 LYS C  110  LEU C  132  1                                  23    
HELIX   12  12 PRO C  137  LEU C  159  1                                  23    
HELIX   13  13 SER D  529  GLY D  559  1                                  31    
HELIX   14  14 PRO D  609  ALA D  611  5                                   3    
HELIX   15  15 LYS D  620  CYS D  622  5                                   3    
HELIX   16  16 ASP D  658  LEU D  673  1                                  16    
HELIX   17  17 SER D  679  LEU D  699  1                                  21    
HELIX   18  18 ASP D  700  GLU D  702  5                                   3    
SHEET    1   A 4 ARG A   5  LYS A   6  0                                        
SHEET    2   A 4 VAL A  34  CYS A  41 -1  O  THR A  40   N  ARG A   5           
SHEET    3   A 4 TRP A  44  LEU A  49 -1  O  ARG A  46   N  GLN A  38           
SHEET    4   A 4 HIS A  52  PRO A  60 -1  O  PHE A  59   N  TYR A  45           
SHEET    1   B 4 ARG A   5  LYS A   6  0                                        
SHEET    2   B 4 VAL A  34  CYS A  41 -1  O  THR A  40   N  ARG A   5           
SHEET    3   B 4 HIS A  12  ALA A  15 -1  N  GLY A  13   O  VAL A  35           
SHEET    4   B 4 ILE A  64  LYS A  67 -1  O  HIS A  65   N  VAL A  14           
SHEET    1   C 4 THR B 560  ARG B 563  0                                        
SHEET    2   C 4 PHE B 574  LEU B 579 -1  O  TRP B 575   N  PHE B 562           
SHEET    3   C 4 VAL B 585  ASP B 590 -1  O  HIS B 587   N  ARG B 578           
SHEET    4   C 4 LYS B 607  PRO B 609 -1  O  LEU B 608   N  LEU B 586           
SHEET    1   D 3 ILE B 613  THR B 618  0                                        
SHEET    2   D 3 ALA B 641  TYR B 646 -1  O  SER B 643   N  VAL B 617           
SHEET    3   D 3 CYS B 650  ILE B 655 -1  O  LEU B 652   N  ILE B 644           
SHEET    1   E 4 ARG C   5  LYS C   6  0                                        
SHEET    2   E 4 VAL C  34  CYS C  41 -1  O  THR C  40   N  ARG C   5           
SHEET    3   E 4 TRP C  44  LEU C  49 -1  O  TYR C  48   N  ARG C  36           
SHEET    4   E 4 HIS C  52  PRO C  60 -1  O  PHE C  59   N  TYR C  45           
SHEET    1   F 4 ARG C   5  LYS C   6  0                                        
SHEET    2   F 4 VAL C  34  CYS C  41 -1  O  THR C  40   N  ARG C   5           
SHEET    3   F 4 HIS C  12  ALA C  15 -1  N  GLY C  13   O  VAL C  35           
SHEET    4   F 4 ILE C  64  LYS C  67 -1  O  HIS C  65   N  VAL C  14           
SHEET    1   G 3 THR D 560  CYS D 561  0                                        
SHEET    2   G 3 TYR D 576  LEU D 579 -1  O  CYS D 577   N  THR D 560           
SHEET    3   G 3 LEU D 586  GLY D 589 -1  O  HIS D 587   N  ARG D 578           
SHEET    1   H 3 ILE D 613  THR D 618  0                                        
SHEET    2   H 3 ALA D 641  TYR D 646 -1  O  SER D 643   N  VAL D 617           
SHEET    3   H 3 CYS D 650  ILE D 655 -1  O  LEU D 652   N  ILE D 644           
LINK         C   GLY A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   ALA A   2     1555   1555  1.33  
LINK         C   LYS A  53                 N   MSE A  54     1555   1555  1.33  
LINK         C   MSE A  54                 N   LEU A  55     1555   1555  1.33  
LINK         C   SER A 119                 N   MSE A 120     1555   1555  1.33  
LINK         C   MSE A 120                 N   MSE A 121     1555   1555  1.33  
LINK         C   MSE A 121                 N   TYR A 122     1555   1555  1.34  
LINK         C   LEU A 124                 N   MSE A 125     1555   1555  1.33  
LINK         C   MSE A 125                 N   GLU A 126     1555   1555  1.33  
LINK         C   HIS B 624                 N   MSE B 625     1555   1555  1.33  
LINK         C   ASP B 676                 N   MSE B 677     1555   1555  1.33  
LINK         C   MSE B 677                 N   MSE B 678     1555   1555  1.33  
LINK         C   MSE B 678                 N   SER B 679     1555   1555  1.33  
LINK         C   SER B 691                 N   MSE B 692     1555   1555  1.33  
LINK         C   MSE B 692                 N   GLU B 693     1555   1555  1.33  
LINK         C   GLY C   0                 N   MSE C   1     1555   1555  1.33  
LINK         C   MSE C   1                 N   ALA C   2     1555   1555  1.32  
LINK         C   LYS C  53                 N   MSE C  54     1555   1555  1.33  
LINK         C   MSE C  54                 N   LEU C  55     1555   1555  1.33  
LINK         C   SER C 119                 N   MSE C 120     1555   1555  1.33  
LINK         C   MSE C 120                 N   MSE C 121     1555   1555  1.33  
LINK         C   MSE C 121                 N   TYR C 122     1555   1555  1.33  
LINK         C   LEU C 124                 N   MSE C 125     1555   1555  1.33  
LINK         C   MSE C 125                 N   GLU C 126     1555   1555  1.33  
LINK         C   HIS D 624                 N   MSE D 625     1555   1555  1.33  
LINK         C   ASP D 676                 N   MSE D 677     1555   1555  1.33  
LINK         C   MSE D 677                 N   MSE D 678     1555   1555  1.33  
LINK         C   MSE D 678                 N   SER D 679     1555   1555  1.33  
LINK         C   SER D 691                 N   MSE D 692     1555   1555  1.32  
LINK         C   MSE D 692                 N   GLU D 693     1555   1555  1.33  
CISPEP   1 ALA A   24    PRO A   25          0         0.63                     
CISPEP   2 ALA C   24    PRO C   25          0         0.39                     
CRYST1   63.837  104.028  124.731  90.00  90.00  90.00 P 21 21 21    8          
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      0.015665  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009613  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008017        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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