GenomeNet

Database: PDB
Entry: 2XY9
LinkDB: 2XY9
Original site: 2XY9 
HEADER    HYDROLASE                               16-NOV-10   2XY9              
TITLE     HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH                   
TITLE    2 PHOSPHINIC TRIPEPTIDE                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 71-654;                                           
COMPND   5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143;     
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_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: CHINESE HAMSTER OVARY CELLS;            
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PLEN/PEE14                                
KEYWDS    HYDROLASE, ZINC METALLOPROTEASE, METALLOPEPTIDASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.AKIF,S.L.SCHWAGER,C.S.ANTHONY,B.CZARNY,F.BEAU,V.DIVE,E.D.STURROCK,  
AUTHOR   2 K.R.ACHARYA                                                          
REVDAT   2   11-APR-12 2XY9    1       REMARK VERSN                             
REVDAT   1   11-MAY-11 2XY9    0                                                
JRNL        AUTH   M.AKIF,S.L.SCHWAGER,C.S.ANTHONY,B.CZARNY,F.BEAU,V.DIVE,      
JRNL        AUTH 2 E.D.STURROCK,K.R.ACHARYA                                     
JRNL        TITL   NOVEL MECHANISM OF INHIBITION OF HUMAN ANGIOTENSIN-          
JRNL        TITL 2 I-CONVERTING ENZYME (ACE) BY A HIGHLY SPECIFIC PHOSPHINIC    
JRNL        TITL 3 TRIPEPTIDE.                                                  
JRNL        REF    BIOCHEM.J.                    V. 436    53 2011              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   21352096                                                     
JRNL        DOI    10.1042/BJ20102123                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
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) : 1.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.82                          
REMARK   3   NUMBER OF REFLECTIONS             : 45842                          
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) : 0.20055                         
REMARK   3   R VALUE            (WORKING SET) : 0.19889                         
REMARK   3   FREE R VALUE                     : 0.23180                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2442                            
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) : 1.967                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.018                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3176                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.58                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.259                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 144                          
REMARK   3   BIN FREE R VALUE                    : 0.307                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4738                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 187                                     
REMARK   3   SOLVENT ATOMS            : 430                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.5                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.940                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00                                                 
REMARK   3    B22 (A**2) : 0.00                                                 
REMARK   3    B33 (A**2) : 0.00                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.188         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.160         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.846         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5076 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6910 ; 1.203 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   578 ; 5.021 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   244 ;34.804 ;24.180       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   804 ;13.805 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;17.450 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   728 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3908 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2922 ; 0.403 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4711 ; 0.780 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2154 ; 1.076 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2199 ; 1.827 ; 4.500       
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 : 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. RESIDUES 435-438 ARE DISORDERED.                 
REMARK   4                                                                      
REMARK   4 2XY9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-NOV-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-46267.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
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 : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49449                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.97                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 4                                  
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4                                  
REMARK 200  R MERGE FOR SHELL          (I) : 0.31                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1O8A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13.5% PEG4000,50MM SODIUM                
REMARK 280  ACETATE, PH 4.7 AND 0.01MM ZNSO4                                    
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       29.36500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.40750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.04700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.40750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.36500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.04700            
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: PISA                                                  
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 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     SER A   435                                                      
REMARK 465     GLU A   436                                                      
REMARK 465     GLY A   437                                                      
REMARK 465     GLY A   438                                                      
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     ASP A 440    CG   OD1  OD2                                       
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       75.36   -174.87                                   
REMARK 500    GLU A 123     -131.63     47.86                                   
REMARK 500    LYS A 363      -35.63   -135.95                                   
REMARK 500    GLN A 554       -3.96     81.48                                   
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 A1628  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 3ES A1635   OAG                                                    
REMARK 620 2 HIS A 383   NE2 101.5                                              
REMARK 620 3 HIS A 387   NE2  97.3 103.8                                        
REMARK 620 4 GLU A 411   OE1 151.0  91.6 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: [(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-                
REMARK 630  {[(BENZYLOXY)[(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-CARBONYL]        
REMARK 630  -AMINO}ETHYL)PHOSPHINYL]-2-[(3-PHENYLISOXAZOL-5-YL)METHYL]-1        
REMARK 630  -OXO-PROPYL}AMINO)-3-(4-HYDROXY-PHENYL)                             
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     3ES A  1635                                                      
REMARK 630     3ES A  1636                                                      
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP: PHQ PPH 1JQ TYR                                             
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A1634                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3ES A1635                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3ES A1636                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800   109 RESIDUES 1629 TO 1633                                          
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2IUL   RELATED DB: PDB                                   
REMARK 900  HUMAN TACE G13 MUTANT                                               
REMARK 900 RELATED ID: 2IUX   RELATED DB: PDB                                   
REMARK 900  HUMAN TACE MUTANT G1234                                             
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: 2C6F   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I                           
REMARK 900  CONVERTING ENZYME N DOMAIN                                          
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: 1O8A   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN                              
REMARK 900  CONVERING ENZYME (NATIVE).                                          
REMARK 900 RELATED ID: 2C6N   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I                           
REMARK 900  CONVERTING ENZYME N DOMAIN WITH LISINOPRIL                          
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: 2XYD   RELATED DB: PDB                                   
REMARK 900  HUMAN ANGIOTENISN CONVERTING ENZYME N-DOMAIN                        
REMARK 900  IN COMPLEX WITH PHOSPHINIC TRIPEPTIDE                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 UNDERGLYCOSYLATED MUTANT LACKING FIRST 36 N-TERMINAL,                
REMARK 999 CYTOPLASMIC, AND TRANSMEMBRANE DOMAIN RESIDUES.                      
DBREF  2XY9 A   40   623  UNP    P12821   ACE_HUMAN       71    654             
SEQADV 2XY9 ALA A  624  UNP  P12821              EXPRESSION TAG                 
SEQRES   1 A  585  ASP GLU ALA GLU ALA SER LYS PHE VAL GLU GLU TYR ASP          
SEQRES   2 A  585  ARG THR SER GLN VAL VAL TRP ASN GLU TYR ALA GLU ALA          
SEQRES   3 A  585  ASN TRP ASN TYR ASN THR ASN ILE THR THR GLU THR SER          
SEQRES   4 A  585  LYS ILE LEU LEU GLN LYS ASN MET GLN ILE ALA ASN HIS          
SEQRES   5 A  585  THR LEU LYS TYR GLY THR GLN ALA ARG LYS PHE ASP VAL          
SEQRES   6 A  585  ASN GLN LEU GLN ASN THR THR ILE LYS ARG ILE ILE LYS          
SEQRES   7 A  585  LYS VAL GLN ASP LEU GLU ARG ALA ALA LEU PRO ALA GLN          
SEQRES   8 A  585  GLU LEU GLU GLU TYR ASN LYS ILE LEU LEU ASP MET GLU          
SEQRES   9 A  585  THR THR TYR SER VAL ALA THR VAL CYS HIS PRO ASN GLY          
SEQRES  10 A  585  SER CYS LEU GLN LEU GLU PRO ASP LEU THR ASN VAL MET          
SEQRES  11 A  585  ALA THR SER ARG LYS TYR GLU ASP LEU LEU TRP ALA TRP          
SEQRES  12 A  585  GLU GLY TRP ARG ASP LYS ALA GLY ARG ALA ILE LEU GLN          
SEQRES  13 A  585  PHE TYR PRO LYS TYR VAL GLU LEU ILE ASN GLN ALA ALA          
SEQRES  14 A  585  ARG LEU ASN GLY TYR VAL ASP ALA GLY ASP SER TRP ARG          
SEQRES  15 A  585  SER MET TYR GLU THR PRO SER LEU GLU GLN ASP LEU GLU          
SEQRES  16 A  585  ARG LEU PHE GLN GLU LEU GLN PRO LEU TYR LEU ASN LEU          
SEQRES  17 A  585  HIS ALA TYR VAL ARG ARG ALA LEU HIS ARG HIS TYR GLY          
SEQRES  18 A  585  ALA GLN HIS ILE ASN LEU GLU GLY PRO ILE PRO ALA HIS          
SEQRES  19 A  585  LEU LEU GLY ASN MET TRP ALA GLN THR TRP SER ASN ILE          
SEQRES  20 A  585  TYR ASP LEU VAL VAL PRO PHE PRO SER ALA PRO SER MET          
SEQRES  21 A  585  ASP THR THR GLU ALA MET LEU LYS GLN GLY TRP THR PRO          
SEQRES  22 A  585  ARG ARG MET PHE LYS GLU ALA ASP ASP PHE PHE THR SER          
SEQRES  23 A  585  LEU GLY LEU LEU PRO VAL PRO PRO GLU PHE TRP ASN LYS          
SEQRES  24 A  585  SER MET LEU GLU LYS PRO THR ASP GLY ARG GLU VAL VAL          
SEQRES  25 A  585  CYS HIS ALA SER ALA TRP ASP PHE TYR ASN GLY LYS ASP          
SEQRES  26 A  585  PHE ARG ILE LYS GLN CYS THR THR VAL ASN LEU GLU ASP          
SEQRES  27 A  585  LEU VAL VAL ALA HIS HIS GLU MET GLY HIS ILE GLN TYR          
SEQRES  28 A  585  PHE MET GLN TYR LYS ASP LEU PRO VAL ALA LEU ARG GLU          
SEQRES  29 A  585  GLY ALA ASN PRO GLY PHE HIS GLU ALA ILE GLY ASP VAL          
SEQRES  30 A  585  LEU ALA LEU SER VAL SER THR PRO LYS HIS LEU HIS SER          
SEQRES  31 A  585  LEU ASN LEU LEU SER SER GLU GLY GLY SER ASP GLU HIS          
SEQRES  32 A  585  ASP ILE ASN PHE LEU MET LYS MET ALA LEU ASP LYS ILE          
SEQRES  33 A  585  ALA PHE ILE PRO PHE SER TYR LEU VAL ASP GLN TRP ARG          
SEQRES  34 A  585  TRP ARG VAL PHE ASP GLY SER ILE THR LYS GLU ASN TYR          
SEQRES  35 A  585  ASN GLN GLU TRP TRP SER LEU ARG LEU LYS TYR GLN GLY          
SEQRES  36 A  585  LEU CYS PRO PRO VAL PRO ARG THR GLN GLY ASP PHE ASP          
SEQRES  37 A  585  PRO GLY ALA LYS PHE HIS ILE PRO SER SER VAL PRO TYR          
SEQRES  38 A  585  ILE ARG TYR PHE VAL SER PHE ILE ILE GLN PHE GLN PHE          
SEQRES  39 A  585  HIS GLU ALA LEU CYS GLN ALA ALA GLY HIS THR GLY PRO          
SEQRES  40 A  585  LEU HIS LYS CYS ASP ILE TYR GLN SER LYS GLU ALA GLY          
SEQRES  41 A  585  GLN ARG LEU ALA THR ALA MET LYS LEU GLY PHE SER ARG          
SEQRES  42 A  585  PRO TRP PRO GLU ALA MET GLN LEU ILE THR GLY GLN PRO          
SEQRES  43 A  585  ASN MET SER ALA SER ALA MET LEU SER TYR PHE LYS PRO          
SEQRES  44 A  585  LEU LEU ASP TRP LEU ARG THR GLU ASN GLU LEU HIS GLY          
SEQRES  45 A  585  GLU LYS LEU GLY TRP PRO GLN TYR ASN TRP THR PRO ALA          
HET    ACT  A1625       4                                                       
HET     CL  A1626       1                                                       
HET     CL  A1627       1                                                       
HET     ZN  A1628       1                                                       
HET    NAG  A1629      14                                                       
HET    NAG  A1630      14                                                       
HET    NAG  A1631      14                                                       
HET    FUC  A1632      10                                                       
HET    BMA  A1633      11                                                       
HET    EPE  A1634      33                                                       
HET    3ES  A1635      51                                                       
HET    3ES  A1636      51                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE                                  
HETNAM   2 EPE  ETHANESULFONIC ACID                                             
HETNAM     3ES [(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-                           
HETNAM   2 3ES  {[(BENZYLOXY)[(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-             
HETNAM   3 3ES  CARBONYL]-AMINO}ETHYL)PHOSPHINYL]-2-[(3-                        
HETNAM   4 3ES  PHENYLISOXAZOL-5-YL)METHYL]-1-OXO-PROPYL}AMINO)-3-              
HETNAM   5 3ES  (4-HYDROXY-PHENYL)                                              
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE                                  
HETNAM   2 EPE  ETHANESULFONIC ACID                                             
HETSYN     EPE HEPES                                                            
FORMUL   2  ACT    C2 H3 O2 1-                                                  
FORMUL   7   CL    2(CL 1-)                                                     
FORMUL   6   ZN    ZN 2+                                                        
FORMUL   5  NAG    3(C8 H15 N O6)                                               
FORMUL   8  FUC    C6 H12 O5                                                    
FORMUL   9  BMA    C6 H12 O6                                                    
FORMUL   3  3ES    2(C38 H38 N3 O9 P)                                           
FORMUL   4  EPE    C8 H18 N2 O4 S                                               
FORMUL  10  HOH   *430(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 ASP A  103  LEU A  107  5                                   5    
HELIX    4   4 ASN A  109  ASP A  121  1                                  13    
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  ALA A  189  1                                  16    
HELIX    9   9 ALA A  189  LEU A  194  1                                   6    
HELIX   10  10 PHE A  196  ASN A  211  1                                  16    
HELIX   11  11 ASP A  215  MET A  223  1                                   9    
HELIX   12  12 SER A  228  LEU A  240  1                                  13    
HELIX   13  13 LEU A  240  GLY A  260  1                                  21    
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  ILE A  455  1                                  17    
HELIX   24  24 ALA A  456  ASP A  473  1                                  18    
HELIX   25  25 ASN A  480  GLY A  494  1                                  15    
HELIX   26  26 PHE A  506  LYS A  511  5                                   6    
HELIX   27  27 TYR A  520  ALA A  541  1                                  22    
HELIX   28  28 PRO A  546  CYS A  550  5                                   5    
HELIX   29  29 SER A  555  LYS A  567  1                                  13    
HELIX   30  30 PRO A  573  GLY A  583  1                                  11    
HELIX   31  31 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  2.29  
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.04  
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.03  
LINK         ND2 ASN A  72                 C1  NAG A1631     1555   1555  1.45  
LINK         ND2 ASN A 109                 C1  NAG A1629     1555   1555  1.44  
LINK        ZN    ZN A1628                 NE2 HIS A 387     1555   1555  2.02  
LINK        ZN    ZN A1628                 OE1 GLU A 411     1555   1555  1.96  
LINK        ZN    ZN A1628                 NE2 HIS A 383     1555   1555  2.02  
LINK        ZN    ZN A1628                 OAG 3ES A1635     1555   1555  2.04  
LINK         O6  NAG A1629                 C1  FUC A1632     1555   1555  1.44  
LINK         O4  NAG A1629                 C1  NAG A1630     1555   1555  1.45  
LINK         O4  NAG A1630                 C1  BMA A1633     1555   1555  1.45  
CISPEP   1 GLU A  162    PRO A  163          0         3.25                     
SITE     1 AC1  7 ASP A 121  GLU A 123  ALA A 208  ASN A 211                    
SITE     2 AC1  7 SER A 219  HOH A2421  HOH A2422                               
SITE     1 AC2  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 AC3  4 TYR A 224  PRO A 519  ARG A 522  HOH A2178                    
SITE     1 AC4  4 HIS A 383  HIS A 387  GLU A 411  3ES A1635                    
SITE     1 AC5  6 ASP A  52  ASP A 396  LEU A 397  PRO A 398                    
SITE     2 AC5  6 ARG A 402  BMA A1633                                          
SITE     1 AC6 27 GLN A 281  HIS A 353  ALA A 354  SER A 355                    
SITE     2 AC6 27 ALA A 356  GLU A 376  VAL A 380  HIS A 383                    
SITE     3 AC6 27 GLU A 384  HIS A 387  PHE A 391  HIS A 410                    
SITE     4 AC6 27 GLU A 411  PHE A 457  LYS A 511  PHE A 512                    
SITE     5 AC6 27 HIS A 513  VAL A 518  TYR A 520  TYR A 523                    
SITE     6 AC6 27 PHE A 527   ZN A1628  3ES A1636  HOH A2321                    
SITE     7 AC6 27 HOH A2323  HOH A2424  HOH A2425                               
SITE     1 AC7 20 TRP A  59  TYR A  62  ASN A  66  GLU A 123                    
SITE     2 AC7 20 ARG A 124  TRP A 220  MET A 223  TRP A 357                    
SITE     3 AC7 20 TYR A 360  GLU A 403  SER A 517  PRO A 519                    
SITE     4 AC7 20 ARG A 522  3ES A1635  HOH A2089  HOH A2426                    
SITE     5 AC7 20 HOH A2427  HOH A2428  HOH A2429  HOH A2430                    
SITE     1 AC8  9 SER A  45  GLU A  49  ASN A  72  THR A  74                    
SITE     2 AC8  9 GLU A  76  ASN A 109  SER A 295  ARG A 348                    
SITE     3 AC8  9 EPE A1634                                                     
CRYST1   58.730   86.094  134.815  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      0.017027  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011615  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007418        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system