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Database: PDB
Entry: 1O8A
LinkDB: 1O8A
Original site: 1O8A 
HEADER    METALLOPROTEASE                         26-NOV-02   1O8A              
TITLE     CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME (NATIVE).    
CAVEAT     1O8A    NAG A 695 HAS WRONG CHIRALITY AT ATOM C1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 68-656;                                           
COMPND   5 SYNONYM: ACE-T, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II;          
COMPND   6 EC: 3.4.15.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: TESTIS;                                                       
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    METALLOPROTEASE, ACE, PEPTIDYL DIPEPTIDASE, TYPE-I MEMBRANE-ANCHORED  
KEYWDS   2 PROTEIN.                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.NATESH,S.L.U.SCHWAGER,E.D.STURROCK,K.R.ACHARYA                      
REVDAT   5   11-JUL-18 1O8A    1       CAVEAT COMPND JRNL   HET                 
REVDAT   5 2                   1       HETNAM FORMUL LINK   ATOM                
REVDAT   4   24-FEB-09 1O8A    1       VERSN                                    
REVDAT   3   06-MAR-06 1O8A    1       TITLE  REMARK                            
REVDAT   2   11-JUL-03 1O8A    1       JRNL                                     
REVDAT   1   07-FEB-03 1O8A    0                                                
JRNL        AUTH   R.NATESH,S.L.SCHWAGER,E.D.STURROCK,K.R.ACHARYA               
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN ANGIOTENSIN-CONVERTING        
JRNL        TITL 2 ENZYME-LISINOPRIL COMPLEX.                                   
JRNL        REF    NATURE                        V. 421   551 2003              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   12540854                                                     
JRNL        DOI    10.1038/NATURE01370                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 41402                          
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) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1675                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4660                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 504                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.40                          
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
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) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.220                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.35                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.810                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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 : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1O8A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-NOV-02.                  
REMARK 100 THE DEPOSITION ID IS D_1290011783.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.70                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42782                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.4600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.440                              
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: PDB ENTRY 1O86                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000/SODIUM ACETATE., PH 4.70         
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       28.31000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.89500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.53000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.89500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.31000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.53000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 CONVERTS ANGIOTENSIN I TO ANGIOTENSIN II BY RELEASE OF               
REMARK 400  THE TERMINAL HIS-LEU, THIS RESULTS IN AN INCREASE OF THE            
REMARK 400  VASOCONSTRICTOR ACTIVITY OF ANGIOTENSIN. ALSO ABLE TO INACTIVATE    
REMARK 400  BRADYKININ, A POTENT VASODILATOR  AND ACTS ON VARIOUS OTHER         
REMARK 400  OLIGOPEPTIDES WITH FREE C-TERMINUS.                                 
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     LEU A    37                                                      
REMARK 465     VAL A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     SER A   435                                                      
REMARK 465     GLU A   436                                                      
REMARK 465     GLY A   437                                                      
REMARK 465     GLY A   438                                                      
REMARK 465     TYR A   619                                                      
REMARK 465     ASN A   620                                                      
REMARK 465     TRP A   621                                                      
REMARK 465     THR A   622                                                      
REMARK 465     PRO A   623                                                      
REMARK 465     ASN A   624                                                      
REMARK 465     SER A   625                                                      
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     ASP A  40    CG   OD1  OD2                                       
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 117    CG   CD   CE   NZ                                   
REMARK 470     SER A 298    OG                                                  
REMARK 470     GLU A 303    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 307    CG   CD   CE   NZ                                   
REMARK 470     SER A 439    CB   OG                                             
REMARK 470     ASP A 440    CG   OD1  OD2                                       
REMARK 470     GLN A 618    CA   C    O    CB   CG   CD   OE1                   
REMARK 470     GLN A 618    NE2                                                 
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  72       76.67   -169.41                                   
REMARK 500    GLU A 123     -136.53     49.77                                   
REMARK 500    GLN A 308       33.14    -97.76                                   
REMARK 500    ASP A 346       -6.67    -53.05                                   
REMARK 500    LYS A 363      -39.81   -133.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 387   NE2                                                    
REMARK 620 2 GLU A 411   OE1 105.0                                              
REMARK 620 3 ACT A 700   OXT  89.5 153.1                                        
REMARK 620 4 ACT A 700   O   127.5  95.5  58.2                                  
REMARK 620 5 HIS A 383   NE2 106.6  95.6 101.8 118.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 691                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 692                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 693                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 694                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 696                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 695                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NXA A 702                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1O86   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX  
REMARK 900 WITH LISINOPRIL.                                                     
DBREF  1O8A A   37   625  UNP    P22966   ACET_HUMAN      68    656             
SEQRES   1 A  589  LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL GLU          
SEQRES   2 A  589  GLU TYR ASP ARG THR SER GLN VAL VAL TRP ASN GLU TYR          
SEQRES   3 A  589  ALA GLU ALA ASN TRP ASN TYR ASN THR ASN ILE THR THR          
SEQRES   4 A  589  GLU THR SER LYS ILE LEU LEU GLN LYS ASN MET GLN ILE          
SEQRES   5 A  589  ALA ASN HIS THR LEU LYS TYR GLY THR GLN ALA ARG LYS          
SEQRES   6 A  589  PHE ASP VAL ASN GLN LEU GLN ASN THR THR ILE LYS ARG          
SEQRES   7 A  589  ILE ILE LYS LYS VAL GLN ASP LEU GLU ARG ALA ALA LEU          
SEQRES   8 A  589  PRO ALA GLN GLU LEU GLU GLU TYR ASN LYS ILE LEU LEU          
SEQRES   9 A  589  ASP MET GLU THR THR TYR SER VAL ALA THR VAL CYS HIS          
SEQRES  10 A  589  PRO ASN GLY SER CYS LEU GLN LEU GLU PRO ASP LEU THR          
SEQRES  11 A  589  ASN VAL MET ALA THR SER ARG LYS TYR GLU ASP LEU LEU          
SEQRES  12 A  589  TRP ALA TRP GLU GLY TRP ARG ASP LYS ALA GLY ARG ALA          
SEQRES  13 A  589  ILE LEU GLN PHE TYR PRO LYS TYR VAL GLU LEU ILE ASN          
SEQRES  14 A  589  GLN ALA ALA ARG LEU ASN GLY TYR VAL ASP ALA GLY ASP          
SEQRES  15 A  589  SER TRP ARG SER MET TYR GLU THR PRO SER LEU GLU GLN          
SEQRES  16 A  589  ASP LEU GLU ARG LEU PHE GLN GLU LEU GLN PRO LEU TYR          
SEQRES  17 A  589  LEU ASN LEU HIS ALA TYR VAL ARG ARG ALA LEU HIS ARG          
SEQRES  18 A  589  HIS TYR GLY ALA GLN HIS ILE ASN LEU GLU GLY PRO ILE          
SEQRES  19 A  589  PRO ALA HIS LEU LEU GLY ASN MET TRP ALA GLN THR TRP          
SEQRES  20 A  589  SER ASN ILE TYR ASP LEU VAL VAL PRO PHE PRO SER ALA          
SEQRES  21 A  589  PRO SER MET ASP THR THR GLU ALA MET LEU LYS GLN GLY          
SEQRES  22 A  589  TRP THR PRO ARG ARG MET PHE LYS GLU ALA ASP ASP PHE          
SEQRES  23 A  589  PHE THR SER LEU GLY LEU LEU PRO VAL PRO PRO GLU PHE          
SEQRES  24 A  589  TRP ASN LYS SER MET LEU GLU LYS PRO THR ASP GLY ARG          
SEQRES  25 A  589  GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR ASN          
SEQRES  26 A  589  GLY LYS ASP PHE ARG ILE LYS GLN CYS THR THR VAL ASN          
SEQRES  27 A  589  LEU GLU ASP LEU VAL VAL ALA HIS HIS GLU MET GLY HIS          
SEQRES  28 A  589  ILE GLN TYR PHE MET GLN TYR LYS ASP LEU PRO VAL ALA          
SEQRES  29 A  589  LEU ARG GLU GLY ALA ASN PRO GLY PHE HIS GLU ALA ILE          
SEQRES  30 A  589  GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO LYS HIS          
SEQRES  31 A  589  LEU HIS SER LEU ASN LEU LEU SER SER GLU GLY GLY SER          
SEQRES  32 A  589  ASP GLU HIS ASP ILE ASN PHE LEU MET LYS MET ALA LEU          
SEQRES  33 A  589  ASP LYS ILE ALA PHE ILE PRO PHE SER TYR LEU VAL ASP          
SEQRES  34 A  589  GLN TRP ARG TRP ARG VAL PHE ASP GLY SER ILE THR LYS          
SEQRES  35 A  589  GLU ASN TYR ASN GLN GLU TRP TRP SER LEU ARG LEU LYS          
SEQRES  36 A  589  TYR GLN GLY LEU CYS PRO PRO VAL PRO ARG THR GLN GLY          
SEQRES  37 A  589  ASP PHE ASP PRO GLY ALA LYS PHE HIS ILE PRO SER SER          
SEQRES  38 A  589  VAL PRO TYR ILE ARG TYR PHE VAL SER PHE ILE ILE GLN          
SEQRES  39 A  589  PHE GLN PHE HIS GLU ALA LEU CYS GLN ALA ALA GLY HIS          
SEQRES  40 A  589  THR GLY PRO LEU HIS LYS CYS ASP ILE TYR GLN SER LYS          
SEQRES  41 A  589  GLU ALA GLY GLN ARG LEU ALA THR ALA MET LYS LEU GLY          
SEQRES  42 A  589  PHE SER ARG PRO TRP PRO GLU ALA MET GLN LEU ILE THR          
SEQRES  43 A  589  GLY GLN PRO ASN MET SER ALA SER ALA MET LEU SER TYR          
SEQRES  44 A  589  PHE LYS PRO LEU LEU ASP TRP LEU ARG THR GLU ASN GLU          
SEQRES  45 A  589  LEU HIS GLY GLU LYS LEU GLY TRP PRO GLN TYR ASN TRP          
SEQRES  46 A  589  THR PRO ASN SER                                              
MODRES 1O8A ASN A   72  ASN  GLYCOSYLATION SITE                                 
MODRES 1O8A ASN A   90  ASN  GLYCOSYLATION SITE                                 
MODRES 1O8A ASN A  109  ASN  GLYCOSYLATION SITE                                 
MODRES 1O8A ASN A  155  ASN  GLYCOSYLATION SITE                                 
MODRES 1O8A ASN A  337  ASN  GLYCOSYLATION SITE                                 
MODRES 1O8A ASN A  586  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 691      14                                                       
HET    NAG  A 692      14                                                       
HET    NAG  A 693      14                                                       
HET    NAG  A 694      14                                                       
HET    NAG  A 695      14                                                       
HET    NAG  A 696      14                                                       
HET    ACT  A 700       4                                                       
HET     ZN  A 701       1                                                       
HET    NXA  A 702       9                                                       
HET     CL  A 703       1                                                       
HET     CL  A 704       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     ACT ACETATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     NXA N-CARBOXYALANINE                                                 
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2  NAG    6(C8 H15 N O6)                                               
FORMUL   8  ACT    C2 H3 O2 1-                                                  
FORMUL   9   ZN    ZN 2+                                                        
FORMUL  10  NXA    C4 H7 N O4                                                   
FORMUL  11   CL    2(CL 1-)                                                     
FORMUL  13  HOH   *504(H2 O)                                                    
HELIX    1   1 ASP A   40  THR A   71  1                                  32    
HELIX    2   2 THR A   74  ARG A  100  1                                  27    
HELIX    3   3 LYS A  101  LEU A  107  5                                   7    
HELIX    4   4 ASN A  109  GLN A  120  1                                  12    
HELIX    5   5 LEU A  122  LEU A  127  5                                   6    
HELIX    6   6 PRO A  128  VAL A  148  1                                  21    
HELIX    7   7 PRO A  163  SER A  172  1                                  10    
HELIX    8   8 LYS A  174  LEU A  210  1                                  37    
HELIX    9   9 ASP A  215  SER A  222  1                                   8    
HELIX   10  10 MET A  223  GLU A  225  5                                   3    
HELIX   11  11 SER A  228  GLY A  260  1                                  33    
HELIX   12  12 TRP A  283  ASN A  285  5                                   3    
HELIX   13  13 ILE A  286  VAL A  291  1                                   6    
HELIX   14  14 ASP A  300  GLN A  308  1                                   9    
HELIX   15  15 THR A  311  LEU A  326  1                                  16    
HELIX   16  16 PRO A  332  SER A  339  1                                   8    
HELIX   17  17 ASN A  374  TYR A  394  1                                  21    
HELIX   18  18 PRO A  398  ARG A  402  5                                   5    
HELIX   19  19 ASN A  406  LEU A  430  1                                  25    
HELIX   20  20 SER A  439  ASP A  473  1                                  35    
HELIX   21  21 ASN A  480  GLY A  494  1                                  15    
HELIX   22  22 PHE A  506  LYS A  511  5                                   6    
HELIX   23  23 TYR A  520  ALA A  541  1                                  22    
HELIX   24  24 PRO A  546  CYS A  550  5                                   5    
HELIX   25  25 SER A  555  LEU A  568  1                                  14    
HELIX   26  26 PRO A  573  GLY A  583  1                                  11    
HELIX   27  27 ALA A  589  HIS A  610  1                                  22    
SHEET    1  AA 2 ALA A 149  HIS A 153  0                                        
SHEET    2  AA 2 SER A 157  LEU A 161 -1  O  LEU A 159   N  VAL A 151           
SHEET    1  AB 2 ILE A 270  ALA A 272  0                                        
SHEET    2  AB 2 LEU A 495  CYS A 496  1  N  CYS A 496   O  ILE A 270           
SHEET    1  AC 2 SER A 355  PHE A 359  0                                        
SHEET    2  AC 2 ASP A 364  LYS A 368 -1  O  ARG A 366   N  TRP A 357           
SSBOND   1 CYS A  152    CYS A  158                          1555   1555  2.03  
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.03  
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.03  
LINK         ND2 ASN A  72                 C1  NAG A 691     1555   1555  1.46  
LINK         ND2 ASN A  72                 O5  NAG A 691     1555   1555  1.88  
LINK         ND2 ASN A  90                 C1  NAG A 692     1555   1555  1.45  
LINK         ND2 ASN A 109                 C1  NAG A 693     1555   1555  1.45  
LINK         ND2 ASN A 155                 C1  NAG A 694     1555   1555  1.45  
LINK         ND2 ASN A 337                 C1  NAG A 695     1555   1555  1.46  
LINK         ND2 ASN A 586                 C1  NAG A 696     1555   1555  1.46  
LINK        ZN    ZN A 701                 NE2 HIS A 387     1555   1555  2.06  
LINK        ZN    ZN A 701                 OE1 GLU A 411     1555   1555  1.97  
LINK        ZN    ZN A 701                 OXT ACT A 700     1555   1555  2.60  
LINK        ZN    ZN A 701                 O   ACT A 700     1555   1555  2.06  
LINK        ZN    ZN A 701                 NE2 HIS A 383     1555   1555  2.02  
CISPEP   1 GLU A  162    PRO A  163          0         0.16                     
SITE     1 AC1  5 ASN A  72  THR A  74  GLU A  76  ASP A 346                    
SITE     2 AC1  5 ARG A 348                                                     
SITE     1 AC2  1 ASN A  90                                                     
SITE     1 AC3  2 ASN A 109  ILE A 112                                          
SITE     1 AC4  3 HIS A 153  ASN A 155  SER A 157                               
SITE     1 AC5  4 THR A 502  ASN A 586  HOH A2221  HOH A2503                    
SITE     1 AC6  1 ASN A 337                                                     
SITE     1 AC7  9 ALA A 354  HIS A 383  GLU A 384  HIS A 387                    
SITE     2 AC7  9 GLU A 411  TYR A 523   ZN A 701  NXA A 702                    
SITE     3 AC7  9 HOH A2317                                                     
SITE     1 AC8  4 HIS A 383  HIS A 387  GLU A 411  ACT A 700                    
SITE     1 AC9  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 BC1  6 TYR A 224  PRO A 407  PRO A 519  ILE A 521                    
SITE     2 BC1  6 ARG A 522  HOH A2195                                          
SITE     1 BC2 10 GLN A 281  HIS A 353  GLU A 384  LYS A 511                    
SITE     2 BC2 10 HIS A 513  TYR A 520  TYR A 523  ACT A 700                    
SITE     3 BC2 10 HOH A2424  HOH A2504                                          
CRYST1   56.620   85.060  133.790  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017662  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011756  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007474        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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