GenomeNet

Database: PDB
Entry: 2I4Q
LinkDB: 2I4Q
Original site: 2I4Q 
HEADER    HYDROLASE                               22-AUG-06   2I4Q              
TITLE     HUMAN RENIN/PF02342674 COMPLEX                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RENIN;                                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ANGIOTENSINOGENASE;                                         
COMPND   5 EC: 3.4.23.15;                                                       
COMPND   6 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: REN;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    RENIN INHIBITOR, PROTEIN-LIGAND COMPLEX, HYDROLASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.D.HOLSWORTH,M.JALAIE,E.ZHANG,P.MCCONNELL,I.MOCHALKIN,               
AUTHOR   2 B.C.FINZEL                                                           
REVDAT   3   02-MAR-10 2I4Q    1       JRNL                                     
REVDAT   2   24-FEB-09 2I4Q    1       VERSN                                    
REVDAT   1   24-OCT-06 2I4Q    0                                                
JRNL        AUTH   N.A.POWELL,F.L.CISKE,C.CAI,D.D.HOLSWORTH,K.MENNEN,           
JRNL        AUTH 2 C.A.VAN HUIS,M.JALAIE,J.DAY,M.MASTRONARDI,                   
JRNL        AUTH 3 P.MCCONNELL,I.MOCHALKIN,E.ZHANG,M.J.RYAN,J.BRYANT,           
JRNL        AUTH 4 W.COLLARD,S.FERREIRA,C.GU,R.COLLINS,J.J.EDMUNDS              
JRNL        TITL   RATIONAL DESIGN OF                                           
JRNL        TITL 2 6-(2,4-DIAMINOPYRIMIDINYL)-1,4-BENZOXAZIN-3-ONES AS          
JRNL        TITL 3 SMALL MOLECULE RENIN INHIBITORS.                             
JRNL        REF    BIOORG.MED.CHEM.              V.  15  5912 2007              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   17574423                                                     
JRNL        DOI    10.1016/J.BMC.2007.05.069                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 37709                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1919                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2771                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 160                          
REMARK   3   BIN FREE R VALUE                    : 0.3840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5184                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 190                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.347         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.248         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.169         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.948         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5386 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4732 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7320 ; 1.080 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11024 ; 0.718 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   670 ; 6.581 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   808 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6012 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1120 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   899 ; 0.171 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5375 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3281 ; 0.080 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   162 ; 0.134 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    18 ; 0.212 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   100 ; 0.253 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.142 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3316 ; 0.828 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5364 ; 1.458 ; 3.500       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2070 ; 0.610 ; 2.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1956 ; 1.055 ; 3.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2I4Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039134.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 170                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
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   : 37838                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY                : 2.630                              
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3                           
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       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
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       70.94900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.94900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.94900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.94900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.94900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.94900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       70.94900            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       70.94900            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       70.94900            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       70.94900            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       70.94900            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       70.94900            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       70.94900            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       70.94900            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       70.94900            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       70.94900            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       70.94900            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       70.94900            
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 300 REMARK: THIS ENTRY CONTAINS A DIMER IN THE ASYMMETRIC UNIT THAT      
REMARK 300 CONSTITUTES A BIOLOGICALLY ACTIVE SPECIES                            
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 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 335    O                                                   
REMARK 470     ARG B 335    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ASN B    70     O    LEU B    87              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  12   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 160   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 323   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B 160   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 323   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  70      -62.18   -133.70                                   
REMARK 500    SER A 207       53.64    -98.77                                   
REMARK 500    SER A 208      141.19   -172.29                                   
REMARK 500    ASP A 214      -14.67     77.14                                   
REMARK 500    ALA A 294       34.65    -83.71                                   
REMARK 500    ASN B  70       91.19   -172.27                                   
REMARK 500    MET B 109       89.08   -152.64                                   
REMARK 500    GLN B 165       49.58   -106.91                                   
REMARK 500    ARG B 246      -74.30    -59.85                                   
REMARK 500    LEU B 247      -55.63   -148.39                                   
REMARK 500    ALA B 294       33.08    -86.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 340        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH B 349        DISTANCE =  7.42 ANGSTROMS                       
REMARK 525    HOH A 392        DISTANCE =  7.78 ANGSTROMS                       
REMARK 525    HOH A 400        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH B 404        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A 405        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH B 414        DISTANCE =  5.70 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UA4 B 336                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UA4 A 336                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2G24   RELATED DB: PDB                                   
REMARK 900 KETOPIPERAZINE-BASED RENIN INHIBITORS: OPTIMIZATION OF THE           
REMARK 900 "C" RING                                                             
REMARK 900 RELATED ID: 2G21   RELATED DB: PDB                                   
REMARK 900 KETOPIPERAZINE-BASED RENIN INHIBITORS: OPTIMIZATION OF THE           
REMARK 900 "C" RING                                                             
REMARK 900 RELATED ID: 2G1S   RELATED DB: PDB                                   
REMARK 900 KETOPIPERAZINE-BASED RENIN INHIBITORS: OPTIMIZATION OF THE           
REMARK 900 C RING                                                               
DBREF  2I4Q A    2   335  UNP    P00797   RENI_HUMAN      71    406             
DBREF  2I4Q B    2   335  UNP    P00797   RENI_HUMAN      71    406             
SEQADV 2I4Q ASN A    0  UNP  P00797              CLONING ARTIFACT               
SEQADV 2I4Q THR A    1  UNP  P00797              CLONING ARTIFACT               
SEQADV 2I4Q ASN B    0  UNP  P00797              CLONING ARTIFACT               
SEQADV 2I4Q THR B    1  UNP  P00797              CLONING ARTIFACT               
SEQRES   1 A  336  ASN THR THR SER SER VAL ILE LEU THR ASN TYR MET ASP          
SEQRES   2 A  336  THR GLN TYR TYR GLY GLU ILE GLY ILE GLY THR PRO PRO          
SEQRES   3 A  336  GLN THR PHE LYS VAL VAL PHE ASP THR GLY SER SER ASN          
SEQRES   4 A  336  VAL TRP VAL PRO SER SER LYS CYS SER ARG LEU TYR THR          
SEQRES   5 A  336  ALA CYS VAL TYR HIS LYS LEU PHE ASP ALA SER ASP SER          
SEQRES   6 A  336  SER SER TYR LYS HIS ASN GLY THR GLU LEU THR LEU ARG          
SEQRES   7 A  336  TYR SER THR GLY THR VAL SER GLY PHE LEU SER GLN ASP          
SEQRES   8 A  336  ILE ILE THR VAL GLY GLY ILE THR VAL THR GLN MET PHE          
SEQRES   9 A  336  GLY GLU VAL THR GLU MET PRO ALA LEU PRO PHE MET LEU          
SEQRES  10 A  336  ALA GLU PHE ASP GLY VAL VAL GLY MET GLY PHE ILE GLU          
SEQRES  11 A  336  GLN ALA ILE GLY ARG VAL THR PRO ILE PHE ASP ASN ILE          
SEQRES  12 A  336  ILE SER GLN GLY VAL LEU LYS GLU ASP VAL PHE SER PHE          
SEQRES  13 A  336  TYR TYR ASN ARG ASP SER GLU ASN SER GLN SER LEU GLY          
SEQRES  14 A  336  GLY GLN ILE VAL LEU GLY GLY SER ASP PRO GLN HIS TYR          
SEQRES  15 A  336  GLU GLY ASN PHE HIS TYR ILE ASN LEU ILE LYS THR GLY          
SEQRES  16 A  336  VAL TRP GLN ILE GLN MET LYS GLY VAL SER VAL GLY SER          
SEQRES  17 A  336  SER THR LEU LEU CYS GLU ASP GLY CYS LEU ALA LEU VAL          
SEQRES  18 A  336  ASP THR GLY ALA SER TYR ILE SER GLY SER THR SER SER          
SEQRES  19 A  336  ILE GLU LYS LEU MET GLU ALA LEU GLY ALA LYS LYS ARG          
SEQRES  20 A  336  LEU PHE ASP TYR VAL VAL LYS CYS ASN GLU GLY PRO THR          
SEQRES  21 A  336  LEU PRO ASP ILE SER PHE HIS LEU GLY GLY LYS GLU TYR          
SEQRES  22 A  336  THR LEU THR SER ALA ASP TYR VAL PHE GLN GLU SER TYR          
SEQRES  23 A  336  SER SER LYS LYS LEU CYS THR LEU ALA ILE HIS ALA MET          
SEQRES  24 A  336  ASP ILE PRO PRO PRO THR GLY PRO THR TRP ALA LEU GLY          
SEQRES  25 A  336  ALA THR PHE ILE ARG LYS PHE TYR THR GLU PHE ASP ARG          
SEQRES  26 A  336  ARG ASN ASN ARG ILE GLY PHE ALA LEU ALA ARG                  
SEQRES   1 B  336  ASN THR THR SER SER VAL ILE LEU THR ASN TYR MET ASP          
SEQRES   2 B  336  THR GLN TYR TYR GLY GLU ILE GLY ILE GLY THR PRO PRO          
SEQRES   3 B  336  GLN THR PHE LYS VAL VAL PHE ASP THR GLY SER SER ASN          
SEQRES   4 B  336  VAL TRP VAL PRO SER SER LYS CYS SER ARG LEU TYR THR          
SEQRES   5 B  336  ALA CYS VAL TYR HIS LYS LEU PHE ASP ALA SER ASP SER          
SEQRES   6 B  336  SER SER TYR LYS HIS ASN GLY THR GLU LEU THR LEU ARG          
SEQRES   7 B  336  TYR SER THR GLY THR VAL SER GLY PHE LEU SER GLN ASP          
SEQRES   8 B  336  ILE ILE THR VAL GLY GLY ILE THR VAL THR GLN MET PHE          
SEQRES   9 B  336  GLY GLU VAL THR GLU MET PRO ALA LEU PRO PHE MET LEU          
SEQRES  10 B  336  ALA GLU PHE ASP GLY VAL VAL GLY MET GLY PHE ILE GLU          
SEQRES  11 B  336  GLN ALA ILE GLY ARG VAL THR PRO ILE PHE ASP ASN ILE          
SEQRES  12 B  336  ILE SER GLN GLY VAL LEU LYS GLU ASP VAL PHE SER PHE          
SEQRES  13 B  336  TYR TYR ASN ARG ASP SER GLU ASN SER GLN SER LEU GLY          
SEQRES  14 B  336  GLY GLN ILE VAL LEU GLY GLY SER ASP PRO GLN HIS TYR          
SEQRES  15 B  336  GLU GLY ASN PHE HIS TYR ILE ASN LEU ILE LYS THR GLY          
SEQRES  16 B  336  VAL TRP GLN ILE GLN MET LYS GLY VAL SER VAL GLY SER          
SEQRES  17 B  336  SER THR LEU LEU CYS GLU ASP GLY CYS LEU ALA LEU VAL          
SEQRES  18 B  336  ASP THR GLY ALA SER TYR ILE SER GLY SER THR SER SER          
SEQRES  19 B  336  ILE GLU LYS LEU MET GLU ALA LEU GLY ALA LYS LYS ARG          
SEQRES  20 B  336  LEU PHE ASP TYR VAL VAL LYS CYS ASN GLU GLY PRO THR          
SEQRES  21 B  336  LEU PRO ASP ILE SER PHE HIS LEU GLY GLY LYS GLU TYR          
SEQRES  22 B  336  THR LEU THR SER ALA ASP TYR VAL PHE GLN GLU SER TYR          
SEQRES  23 B  336  SER SER LYS LYS LEU CYS THR LEU ALA ILE HIS ALA MET          
SEQRES  24 B  336  ASP ILE PRO PRO PRO THR GLY PRO THR TRP ALA LEU GLY          
SEQRES  25 B  336  ALA THR PHE ILE ARG LYS PHE TYR THR GLU PHE ASP ARG          
SEQRES  26 B  336  ARG ASN ASN ARG ILE GLY PHE ALA LEU ALA ARG                  
HET    UA4  B 336      35                                                       
HET    UA4  A 336      35                                                       
HETNAM     UA4 (2S)-6-(2,4-DIAMINO-6-ETHYLPYRIMIDIN-5-YL)-2-(3,5-               
HETNAM   2 UA4  DIFLUOROPHENYL)-4-(3-METHOXYPROPYL)-2-METHYL-2H-1,4-            
HETNAM   3 UA4  BENZOXAZIN-3(4H)-ONE                                            
FORMUL   3  UA4    2(C25 H27 F2 N5 O3)                                          
FORMUL   5  HOH   *190(H2 O)                                                    
HELIX    1   1 TYR A   50  TYR A   55  1                                   6    
HELIX    2   2 ASP A   60  SER A   64  5                                   5    
HELIX    3   3 PRO A  110  MET A  115  1                                   6    
HELIX    4   4 PHE A  127  VAL A  135  5                                   9    
HELIX    5   5 PRO A  137  SER A  144  1                                   8    
HELIX    6   6 ASP A  177  GLN A  179  5                                   3    
HELIX    7   7 SER A  230  GLY A  242  1                                  13    
HELIX    8   8 ASN A  255  LEU A  260  5                                   6    
HELIX    9   9 THR A  275  VAL A  280  1                                   6    
HELIX   10  10 GLY A  311  LYS A  317  1                                   7    
HELIX   11  11 TYR B   50  TYR B   55  1                                   6    
HELIX   12  12 ASP B   60  SER B   64  5                                   5    
HELIX   13  13 PRO B  110  MET B  115  1                                   6    
HELIX   14  14 PHE B  127  VAL B  135  5                                   9    
HELIX   15  15 PRO B  137  GLN B  145  1                                   9    
HELIX   16  16 ASP B  177  TYR B  181  5                                   5    
HELIX   17  17 SER B  230  GLY B  242  1                                  13    
HELIX   18  18 ASN B  255  LEU B  260  5                                   6    
HELIX   19  19 THR B  275  VAL B  280  1                                   6    
HELIX   20  20 GLY B  311  LYS B  317  1                                   7    
SHEET    1   A 9 LYS A  68  TYR A  78  0                                        
SHEET    2   A 9 GLY A  81  VAL A  94 -1  O  GLN A  89   N  LYS A  68           
SHEET    3   A 9 GLN A  14  ILE A  21 -1  N  GLY A  20   O  THR A  93           
SHEET    4   A 9 SER A   3  TYR A  10 -1  N  THR A   8   O  TYR A  16           
SHEET    5   A 9 GLY A 169  LEU A 173 -1  O  ILE A 171   N  VAL A   5           
SHEET    6   A 9 VAL A 152  TYR A 157 -1  N  TYR A 156   O  GLN A 170           
SHEET    7   A 9 PHE A 318  ASP A 323 -1  O  PHE A 322   N  PHE A 153           
SHEET    8   A 9 ARG A 328  ALA A 334 -1  O  GLY A 330   N  GLU A 321           
SHEET    9   A 9 TYR A 181  ASN A 189 -1  N  ILE A 188   O  ILE A 329           
SHEET    1   B13 LYS A  68  TYR A  78  0                                        
SHEET    2   B13 GLY A  81  VAL A  94 -1  O  GLN A  89   N  LYS A  68           
SHEET    3   B13 ILE A  97  GLU A 108 -1  O  GLU A 105   N  PHE A  86           
SHEET    4   B13 VAL A  39  PRO A  42  1  N  VAL A  39   O  GLY A 104           
SHEET    5   B13 GLY A 121  GLY A 124 -1  O  VAL A 122   N  TRP A  40           
SHEET    6   B13 GLN A  26  ASP A  33  1  N  VAL A  31   O  VAL A 123           
SHEET    7   B13 GLN A  14  ILE A  21 -1  N  GLY A  17   O  VAL A  30           
SHEET    8   B13 SER A   3  TYR A  10 -1  N  THR A   8   O  TYR A  16           
SHEET    9   B13 GLY A 169  LEU A 173 -1  O  ILE A 171   N  VAL A   5           
SHEET   10   B13 VAL A 152  TYR A 157 -1  N  TYR A 156   O  GLN A 170           
SHEET   11   B13 PHE A 318  ASP A 323 -1  O  PHE A 322   N  PHE A 153           
SHEET   12   B13 ARG A 328  ALA A 334 -1  O  GLY A 330   N  GLU A 321           
SHEET   13   B13 TYR A 181  ASN A 189 -1  N  ILE A 188   O  ILE A 329           
SHEET    1   C 5 GLN A 197  MET A 200  0                                        
SHEET    2   C 5 CYS A 216  VAL A 220 -1  O  ALA A 218   N  ILE A 198           
SHEET    3   C 5 TRP A 308  LEU A 310  1  O  LEU A 310   N  LEU A 219           
SHEET    4   C 5 ILE A 227  GLY A 229 -1  N  SER A 228   O  ALA A 309           
SHEET    5   C 5 ILE A 295  ALA A 297  1  O  HIS A 296   N  ILE A 227           
SHEET    1   D 3 GLY A 202  VAL A 205  0                                        
SHEET    2   D 3 ILE A 263  LEU A 267 -1  O  HIS A 266   N  GLY A 202           
SHEET    3   D 3 LYS A 270  LEU A 274 -1  O  LEU A 274   N  ILE A 263           
SHEET    1   E 3 LYS A 244  LYS A 245  0                                        
SHEET    2   E 3 TYR A 250  LYS A 253 -1  O  VAL A 251   N  LYS A 244           
SHEET    3   E 3 LEU A 290  THR A 292 -1  O  CYS A 291   N  VAL A 252           
SHEET    1   F 9 LYS B  68  ARG B  77  0                                        
SHEET    2   F 9 THR B  82  VAL B  94 -1  O  VAL B  83   N  LEU B  76           
SHEET    3   F 9 GLN B  14  ILE B  21 -1  N  GLY B  20   O  THR B  93           
SHEET    4   F 9 SER B   3  TYR B  10 -1  N  THR B   8   O  TYR B  16           
SHEET    5   F 9 GLY B 169  LEU B 173 -1  O  LEU B 173   N  SER B   3           
SHEET    6   F 9 VAL B 152  TYR B 157 -1  N  TYR B 156   O  GLN B 170           
SHEET    7   F 9 PHE B 318  ASP B 323 -1  O  PHE B 322   N  PHE B 153           
SHEET    8   F 9 ARG B 328  LEU B 333 -1  O  GLY B 330   N  GLU B 321           
SHEET    9   F 9 HIS B 186  ASN B 189 -1  N  ILE B 188   O  ILE B 329           
SHEET    1   G13 LYS B  68  ARG B  77  0                                        
SHEET    2   G13 THR B  82  VAL B  94 -1  O  VAL B  83   N  LEU B  76           
SHEET    3   G13 ILE B  97  GLU B 108 -1  O  GLU B 105   N  PHE B  86           
SHEET    4   G13 VAL B  39  PRO B  42  1  N  VAL B  41   O  GLY B 104           
SHEET    5   G13 GLY B 121  GLY B 124 -1  O  VAL B 122   N  TRP B  40           
SHEET    6   G13 GLN B  26  ASP B  33  1  N  VAL B  31   O  VAL B 123           
SHEET    7   G13 GLN B  14  ILE B  21 -1  N  GLY B  17   O  VAL B  30           
SHEET    8   G13 SER B   3  TYR B  10 -1  N  THR B   8   O  TYR B  16           
SHEET    9   G13 GLY B 169  LEU B 173 -1  O  LEU B 173   N  SER B   3           
SHEET   10   G13 VAL B 152  TYR B 157 -1  N  TYR B 156   O  GLN B 170           
SHEET   11   G13 PHE B 318  ASP B 323 -1  O  PHE B 322   N  PHE B 153           
SHEET   12   G13 ARG B 328  LEU B 333 -1  O  GLY B 330   N  GLU B 321           
SHEET   13   G13 HIS B 186  ASN B 189 -1  N  ILE B 188   O  ILE B 329           
SHEET    1   H 5 GLN B 197  MET B 200  0                                        
SHEET    2   H 5 CYS B 216  VAL B 220 -1  O  ALA B 218   N  ILE B 198           
SHEET    3   H 5 TRP B 308  LEU B 310  1  O  LEU B 310   N  LEU B 219           
SHEET    4   H 5 ILE B 227  GLY B 229 -1  N  SER B 228   O  ALA B 309           
SHEET    5   H 5 ILE B 295  ALA B 297  1  O  HIS B 296   N  ILE B 227           
SHEET    1   I 3 VAL B 203  VAL B 205  0                                        
SHEET    2   I 3 ILE B 263  LEU B 267 -1  O  SER B 264   N  SER B 204           
SHEET    3   I 3 LYS B 270  LEU B 274 -1  O  LEU B 274   N  ILE B 263           
SHEET    1   J 3 LYS B 244  LYS B 245  0                                        
SHEET    2   J 3 TYR B 250  LYS B 253 -1  O  VAL B 251   N  LYS B 244           
SHEET    3   J 3 LEU B 290  THR B 292 -1  O  CYS B 291   N  VAL B 252           
SSBOND   1 CYS A   46    CYS A   53                          1555   1555  2.02  
SSBOND   2 CYS A  212    CYS A  216                          1555   1555  2.04  
SSBOND   3 CYS A  254    CYS A  291                          1555   1555  2.04  
SSBOND   4 CYS B   46    CYS B   53                          1555   1555  2.03  
SSBOND   5 CYS B  212    CYS B  216                          1555   1555  2.04  
SSBOND   6 CYS B  254    CYS B  291                          1555   1555  2.04  
CISPEP   1 THR A   23    PRO A   24          0        -1.19                     
CISPEP   2 LEU A  112    PRO A  113          0         5.38                     
CISPEP   3 PRO A  302    PRO A  303          0         3.13                     
CISPEP   4 GLY A  305    PRO A  306          0         1.26                     
CISPEP   5 THR B   23    PRO B   24          0        -0.58                     
CISPEP   6 LEU B  112    PRO B  113          0         2.84                     
CISPEP   7 PRO B  302    PRO B  303          0         2.59                     
CISPEP   8 GLY B  305    PRO B  306          0        -7.43                     
SITE     1 AC1 15 THR B  13  GLN B  14  TYR B  15  VAL B  31                    
SITE     2 AC1 15 ASP B  33  TYR B  78  THR B  80  PRO B 113                    
SITE     3 AC1 15 LEU B 116  ALA B 117  ASP B 221  THR B 222                    
SITE     4 AC1 15 GLY B 223  SER B 225  ASN B 255                               
SITE     1 AC2 16 THR A  13  GLN A  14  TYR A  15  VAL A  31                    
SITE     2 AC2 16 ASP A  33  TYR A  55  TYR A  78  SER A  79                    
SITE     3 AC2 16 THR A  80  LEU A 116  ALA A 117  VAL A 122                    
SITE     4 AC2 16 ASP A 221  THR A 222  GLY A 223  SER A 225                    
CRYST1  141.898  141.898  141.898  90.00  90.00  90.00 P 21 3       24          
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      0.007047  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007047  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007047        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system