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Database: PDB
Entry: 2IUX
LinkDB: 2IUX
Original site: 2IUX 
HEADER    HYDROLASE                               07-JUN-06   2IUX              
TITLE     HUMAN TACE MUTANT G1234                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 68-658;                                           
COMPND   5 SYNONYM: HUMAN TACE G1234 MUTANT, TESTIS-SPECIFIC ISOFORM,           
COMPND   6  ACE-T, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II;                  
COMPND   7 EC: 3.2.1.-, 3.4.15.1;                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: CHINESE HAMSTER OVARY CELLS             
KEYWDS    GLYCOSIDASE, POLYMORPHISM, GLYCOPROTEIN, METAL-BINDING,               
KEYWDS   2 ALTERNATIVE SPLICING, METALLOPROTEASE, PHOSPHORYLATION,              
KEYWDS   3 AC, ZINC, MEMBRANE, CHLORIDE, PROTEASE, HYDROLASE, TYPE-I            
KEYWDS   4 MEMBRANE-ANCHORED PROTEIN, CARBOXYPEPTIDASE, PEPTIDYL                
KEYWDS   5 DIPEPTIDASE, TRANSMEMBRANE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.WATERMEYER,B.T.SWELL,R.NATESH,H.R.CORRADI,K.R.ACHARYA,            
AUTHOR   2 E.D.STURROCK                                                         
REVDAT   2   24-FEB-09 2IUX    1       VERSN                                    
REVDAT   1   25-OCT-06 2IUX    0                                                
JRNL        AUTH   J.M.WATERMEYER,B.T.SEWELL,S.L.SCHWAGER,R.NATESH,             
JRNL        AUTH 2 H.R.CORRADI,K.R.ACHARYA,E.D.STURROCK                         
JRNL        TITL   STRUCTURE OF TESTIS ACE GLYCOSYLATION MUTANTS AND            
JRNL        TITL 2 EVIDENCE FOR CONSERVED DOMAIN MOVEMENT.                      
JRNL        REF    BIOCHEMISTRY                  V.  45 12654 2006              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   17042482                                                     
JRNL        DOI    10.1021/BI061146Z                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.8  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 : MLF                                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.8                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 13572                          
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) : 0.2006                          
REMARK   3   FREE R VALUE                     : 0.2369                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.4                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1379                            
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            : 4696                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 33                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20                             
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.46                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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        : 0.361842                                             
REMARK   3   BSOL        : 14.8386                                              
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  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2IUX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  08-JUN-06.                 
REMARK 100 THE PDBE ID CODE IS EBI-29018.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13572                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.6                               
REMARK 200  DATA REDUNDANCY                : 39.000                             
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
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  (%): 48.32                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH4.7 15%            
REMARK 280  PEG 4000, 10UM ZINC SULPHATE                                        
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       28.21800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.71200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.57450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.71200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.21800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.57450            
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 GENERATING THE BIOMOLECULE                                           
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 ENGINEERED RESIDUE IN CHAIN A, ASN 368 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 617 TO GLN                        
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     GLU A   436                                                      
REMARK 465     GLN A   618                                                      
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 465     ALA A   626                                                      
REMARK 465     ARG A   627                                                      
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     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     SER A 298    OG                                                  
REMARK 470     LYS A 307    CG   CD   CE   NZ                                   
REMARK 470     LYS A 363    CE   NZ                                             
REMARK 470     LYS A 425    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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       82.49   -171.76                                   
REMARK 500    ARG A 100       -9.83    -58.89                                   
REMARK 500    ASN A 105        1.18    -67.67                                   
REMARK 500    GLU A 123     -135.55     50.21                                   
REMARK 500    ASP A 164      -74.82    -44.48                                   
REMARK 500    ALA A 272      -17.39    -47.81                                   
REMARK 500    MET A 278      -38.65    -36.38                                   
REMARK 500    ARG A 348      150.07    -46.91                                   
REMARK 500    LYS A 363      -32.71   -144.75                                   
REMARK 500    ASP A 453      -61.07    -91.69                                   
REMARK 500    HIS A 513      -18.41    -46.31                                   
REMARK 500    TRP A 616     -157.43   -127.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS A  153     PRO A  154                  133.82                    
REMARK 500 PRO A  154     ASN A  155                  143.63                    
REMARK 500 PHE A  196     TYR A  197                 -145.98                    
REMARK 500 GLN A  584     PRO A  585                 -147.02                    
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 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 A1621  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 383   NE2                                                    
REMARK 620 2 HIS A 387   NE2  97.2                                              
REMARK 620 3 GLU A 411   OE1  91.6 114.5                                        
REMARK 620 4 ACT A1620   O   106.0 100.9 138.1                                  
REMARK 620 5 ACT A1620   OXT 129.0 127.8  90.1  49.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NXA A1624                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1O86   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN                              
REMARK 900  CONVERING ENZYME IN COMPLEX WITH LISINOPRIL.                        
REMARK 900 RELATED ID: 1O8A   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN                              
REMARK 900  CONVERING ENZYME (NATIVE).                                          
REMARK 900 RELATED ID: 1UZE   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF THE ANTI-HYPERTENSIVE DRUG                               
REMARK 900  ENALAPRIL AN THE HUMAN TESTICULAR ANGIOTENSIN                       
REMARK 900   I-CONVERTING ENZYME                                                
REMARK 900 RELATED ID: 1UZF   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF THE ANTI-HYPERTENSIVE DRUG                               
REMARK 900  CAPTOPRIL AN THE HUMAN TESTICULAR ANGIOTENSIN                       
REMARK 900   I-CONVERTING ENZYME                                                
REMARK 900 RELATED ID: 2IUL   RELATED DB: PDB                                   
REMARK 900  HUMAN TACE G13 MUTANT                                               
DBREF  2IUX A   37   627  UNP    P22966   ACET_HUMAN      68    658             
SEQADV 2IUX GLN A  337  UNP  P22966    ASN   368 ENGINEERED MUTATION            
SEQADV 2IUX GLN A  586  UNP  P22966    ASN   617 ENGINEERED MUTATION            
SEQRES   1 A  591  LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL GLU          
SEQRES   2 A  591  GLU TYR ASP ARG THR SER GLN VAL VAL TRP ASN GLU TYR          
SEQRES   3 A  591  ALA GLU ALA ASN TRP ASN TYR ASN THR ASN ILE THR THR          
SEQRES   4 A  591  GLU THR SER LYS ILE LEU LEU GLN LYS ASN MET GLN ILE          
SEQRES   5 A  591  ALA ASN HIS THR LEU LYS TYR GLY THR GLN ALA ARG LYS          
SEQRES   6 A  591  PHE ASP VAL ASN GLN LEU GLN ASN THR THR ILE LYS ARG          
SEQRES   7 A  591  ILE ILE LYS LYS VAL GLN ASP LEU GLU ARG ALA ALA LEU          
SEQRES   8 A  591  PRO ALA GLN GLU LEU GLU GLU TYR ASN LYS ILE LEU LEU          
SEQRES   9 A  591  ASP MET GLU THR THR TYR SER VAL ALA THR VAL CYS HIS          
SEQRES  10 A  591  PRO ASN GLY SER CYS LEU GLN LEU GLU PRO ASP LEU THR          
SEQRES  11 A  591  ASN VAL MET ALA THR SER ARG LYS TYR GLU ASP LEU LEU          
SEQRES  12 A  591  TRP ALA TRP GLU GLY TRP ARG ASP LYS ALA GLY ARG ALA          
SEQRES  13 A  591  ILE LEU GLN PHE TYR PRO LYS TYR VAL GLU LEU ILE ASN          
SEQRES  14 A  591  GLN ALA ALA ARG LEU ASN GLY TYR VAL ASP ALA GLY ASP          
SEQRES  15 A  591  SER TRP ARG SER MET TYR GLU THR PRO SER LEU GLU GLN          
SEQRES  16 A  591  ASP LEU GLU ARG LEU PHE GLN GLU LEU GLN PRO LEU TYR          
SEQRES  17 A  591  LEU ASN LEU HIS ALA TYR VAL ARG ARG ALA LEU HIS ARG          
SEQRES  18 A  591  HIS TYR GLY ALA GLN HIS ILE ASN LEU GLU GLY PRO ILE          
SEQRES  19 A  591  PRO ALA HIS LEU LEU GLY ASN MET TRP ALA GLN THR TRP          
SEQRES  20 A  591  SER ASN ILE TYR ASP LEU VAL VAL PRO PHE PRO SER ALA          
SEQRES  21 A  591  PRO SER MET ASP THR THR GLU ALA MET LEU LYS GLN GLY          
SEQRES  22 A  591  TRP THR PRO ARG ARG MET PHE LYS GLU ALA ASP ASP PHE          
SEQRES  23 A  591  PHE THR SER LEU GLY LEU LEU PRO VAL PRO PRO GLU PHE          
SEQRES  24 A  591  TRP GLN LYS SER MET LEU GLU LYS PRO THR ASP GLY ARG          
SEQRES  25 A  591  GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR ASN          
SEQRES  26 A  591  GLY LYS ASP PHE ARG ILE LYS GLN CYS THR THR VAL ASN          
SEQRES  27 A  591  LEU GLU ASP LEU VAL VAL ALA HIS HIS GLU MET GLY HIS          
SEQRES  28 A  591  ILE GLN TYR PHE MET GLN TYR LYS ASP LEU PRO VAL ALA          
SEQRES  29 A  591  LEU ARG GLU GLY ALA ASN PRO GLY PHE HIS GLU ALA ILE          
SEQRES  30 A  591  GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO LYS HIS          
SEQRES  31 A  591  LEU HIS SER LEU ASN LEU LEU SER SER GLU GLY GLY SER          
SEQRES  32 A  591  ASP GLU HIS ASP ILE ASN PHE LEU MET LYS MET ALA LEU          
SEQRES  33 A  591  ASP LYS ILE ALA PHE ILE PRO PHE SER TYR LEU VAL ASP          
SEQRES  34 A  591  GLN TRP ARG TRP ARG VAL PHE ASP GLY SER ILE THR LYS          
SEQRES  35 A  591  GLU ASN TYR ASN GLN GLU TRP TRP SER LEU ARG LEU LYS          
SEQRES  36 A  591  TYR GLN GLY LEU CYS PRO PRO VAL PRO ARG THR GLN GLY          
SEQRES  37 A  591  ASP PHE ASP PRO GLY ALA LYS PHE HIS ILE PRO SER SER          
SEQRES  38 A  591  VAL PRO TYR ILE ARG TYR PHE VAL SER PHE ILE ILE GLN          
SEQRES  39 A  591  PHE GLN PHE HIS GLU ALA LEU CYS GLN ALA ALA GLY HIS          
SEQRES  40 A  591  THR GLY PRO LEU HIS LYS CYS ASP ILE TYR GLN SER LYS          
SEQRES  41 A  591  GLU ALA GLY GLN ARG LEU ALA THR ALA MET LYS LEU GLY          
SEQRES  42 A  591  PHE SER ARG PRO TRP PRO GLU ALA MET GLN LEU ILE THR          
SEQRES  43 A  591  GLY GLN PRO GLN MET SER ALA SER ALA MET LEU SER TYR          
SEQRES  44 A  591  PHE LYS PRO LEU LEU ASP TRP LEU ARG THR GLU ASN GLU          
SEQRES  45 A  591  LEU HIS GLY GLU LYS LEU GLY TRP PRO GLN TYR ASN TRP          
SEQRES  46 A  591  THR PRO ASN SER ALA ARG                                      
HET    NAG  A1618      14                                                       
HET    NAG  A1619      14                                                       
HET    ACT  A1620       4                                                       
HET     ZN  A1621       1                                                       
HET     CL  A1622       1                                                       
HET     CL  A1623       1                                                       
HET    NXA  A1624       9                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     ACT ACETATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     NXA N-CARBOXYALANINE                                                 
HETSYN     NAG NAG                                                              
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL   8  NXA    C4 H7 N O4                                                   
FORMUL   9  HOH   *33(H2 O1)                                                    
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 ASP A  103  LEU A  107  5                                   5    
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  ALA A  149  1                                  22    
HELIX    7   7 PRO A  163  SER A  172  1                                  10    
HELIX    8   8 LYS A  174  GLN A  195  1                                  22    
HELIX    9   9 PHE A  196  LEU A  210  1                                  15    
HELIX   10  10 ASP A  215  MET A  223  1                                   9    
HELIX   11  11 SER A  228  LEU A  240  1                                  13    
HELIX   12  12 LEU A  240  GLY A  260  1                                  21    
HELIX   13  13 HIS A  273  LEU A  275  5                                   3    
HELIX   14  14 TRP A  283  ASN A  285  5                                   3    
HELIX   15  15 ILE A  286  VAL A  291  1                                   6    
HELIX   16  16 ASP A  300  GLN A  308  1                                   9    
HELIX   17  17 THR A  311  LEU A  326  1                                  16    
HELIX   18  18 PRO A  332  SER A  339  1                                   8    
HELIX   19  19 ASN A  374  TYR A  394  1                                  21    
HELIX   20  20 PRO A  398  ARG A  402  5                                   5    
HELIX   21  21 ASN A  406  SER A  422  1                                  17    
HELIX   22  22 THR A  423  LEU A  430  1                                   8    
HELIX   23  23 SER A  439  ASP A  473  1                                  35    
HELIX   24  24 ASN A  480  GLY A  494  1                                  15    
HELIX   25  25 PHE A  506  LYS A  511  5                                   6    
HELIX   26  26 TYR A  520  ALA A  541  1                                  22    
HELIX   27  27 PRO A  546  CYS A  550  5                                   5    
HELIX   28  28 SER A  555  LEU A  568  1                                  14    
HELIX   29  29 PRO A  573  GLY A  583  1                                  11    
HELIX   30  30 ALA A  589  HIS A  610  1                                  22    
SHEET    1  AA 2 THR A 150  CYS A 152  0                                        
SHEET    2  AA 2 CYS A 158  GLN A 160 -1  O  LEU A 159   N  VAL A 151           
SHEET    1  AB 2 ILE A 270  PRO A 271  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  ASP A 358  0                                        
SHEET    2  AC 2 PHE A 365  LYS A 368 -1  O  ARG A 366   N  TRP A 357           
SSBOND   1 CYS A  152    CYS A  158                          1555   1555  2.04  
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 A1618     1555   1555  1.46  
LINK         ND2 ASN A 109                 C1  NAG A1619     1555   1555  1.49  
LINK        ZN    ZN A1621                 O   ACT A1620     1555   1555  2.75  
LINK        ZN    ZN A1621                 NE2 HIS A 387     1555   1555  2.19  
LINK        ZN    ZN A1621                 OE1 GLU A 411     1555   1555  2.21  
LINK        ZN    ZN A1621                 OXT ACT A1620     1555   1555  2.47  
LINK        ZN    ZN A1621                 NE2 HIS A 383     1555   1555  2.21  
CISPEP   1 GLU A  162    PRO A  163          0        -0.24                     
SITE     1 AC1  5 ASN A  72  GLU A  76  THR A  77  ASP A 346                    
SITE     2 AC1  5 ARG A 348                                                     
SITE     1 AC2  2 ASN A 109  ILE A 112                                          
SITE     1 AC3  6 ALA A 354  GLU A 384  GLU A 411  TYR A 523                    
SITE     2 AC3  6  ZN A1621  NXA A1624                                          
SITE     1 AC4  4 HIS A 383  HIS A 387  GLU A 411  ACT A1620                    
SITE     1 AC5  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 AC6  5 TYR A 224  PRO A 407  PRO A 519  ARG A 522                    
SITE     2 AC6  5 HOH A2014                                                     
SITE     1 AC7 10 GLN A 281  HIS A 353  HIS A 383  GLU A 384                    
SITE     2 AC7 10 LYS A 511  HIS A 513  TYR A 520  TYR A 523                    
SITE     3 AC7 10 ACT A1620  HOH A2033                                          
CRYST1   56.436   85.149  133.424  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      0.017719  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011744  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007495        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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