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Database: PDB
Entry: 4APH
LinkDB: 4APH
Original site: 4APH 
HEADER    HYDROLASE/HORMONE                       03-APR-12   4APH              
TITLE     HUMAN ANGIOTENSIN-CONVERTING ENZYME IN COMPLEX WITH ANGIOTENSIN-II    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 68-656;                     
COMPND   5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143,     
COMPND   6  ACE-T;                                                              
COMPND   7 EC: 3.2.1.-, 3.4.15.1;                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ANGIOTENSIN-2;                                             
COMPND  11 CHAIN: P;                                                            
COMPND  12 SYNONYM: ANGIOTENSIN II, ANG II                                      
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_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    HYDROLASE-HORMONE COMPLEX, ZINC METALLOPROTEASE, METALLOPEPTIDASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MASUYER,S.L.U.SCHWAGER,E.D.STURROCK,R.E.ISAAC,K.R.ACHARYA           
REVDAT   3   25-JAN-17 4APH    1       REMARK HETNAM LINK   ATOM                
REVDAT   3 2                           ANISOU CONECT MASTER                     
REVDAT   2   24-OCT-12 4APH    1       JRNL                                     
REVDAT   1   17-OCT-12 4APH    0                                                
JRNL        AUTH   G.MASUYER,S.L.U.SCHWAGER,E.D.STURROCK,R.E.ISAAC,K.R.ACHARYA  
JRNL        TITL   MOLECULAR RECOGNITION AND REGULATION OF HUMAN ANGIOTENSIN-I  
JRNL        TITL 2 CONVERTING ENZYME (ACE) ACTIVITY BY NATURAL INHIBITORY       
JRNL        TITL 3 PEPTIDES.                                                    
JRNL        REF    SCI.REP.                      V.   2   717 2012              
JRNL        REFN                   ISSN 2045-2322                               
JRNL        PMID   23056909                                                     
JRNL        DOI    10.1038/SREP00717                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.43                          
REMARK   3   NUMBER OF REFLECTIONS             : 35133                          
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) : 0.19638                         
REMARK   3   R VALUE            (WORKING SET) : 0.19406                         
REMARK   3   FREE R VALUE                     : 0.24026                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1877                            
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) : 1.990                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.042                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2436                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.258                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 134                          
REMARK   3   BIN FREE R VALUE                    : 0.298                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4944                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 285                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.286                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.54                                                
REMARK   3    B22 (A**2) : -0.84                                                
REMARK   3    B33 (A**2) : 1.38                                                 
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): 0.260         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.202         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.119         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.258         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5187 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7062 ; 1.024 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   610 ; 4.972 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   263 ;34.248 ;24.373       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   839 ;13.799 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;14.989 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   742 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4045 ; 0.004 ; 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):  3047 ; 0.330 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4918 ; 0.653 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2140 ; 1.014 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2144 ; 1.717 ; 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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    40        A   625                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1518  -5.7943 -23.9715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0205 T22:   0.0066                                     
REMARK   3      T33:   0.0145 T12:  -0.0038                                     
REMARK   3      T13:  -0.0043 T23:   0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1938 L22:   0.3240                                     
REMARK   3      L33:   0.3101 L12:  -0.0286                                     
REMARK   3      L13:   0.0057 L23:   0.1779                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0001 S12:  -0.0180 S13:  -0.0079                       
REMARK   3      S21:   0.0145 S22:   0.0116 S23:  -0.0374                       
REMARK   3      S31:   0.0014 S32:  -0.0031 S33:  -0.0117                       
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. TWO DIFFERENT CONFIRMATIONS ARE VISIBLE          
REMARK   3   FOR ANG II (CHAIN P).                                              
REMARK   4                                                                      
REMARK   4 4APH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-51972.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-12                          
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) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS-2M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37104                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.99                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.53                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.9                               
REMARK 200  DATA REDUNDANCY                : 4.7                                
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.70                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.62                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.60                               
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   (%): 49                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM SODIUM ACETATE PH 4.7, 16%          
REMARK 280  PEG4000, 10UM 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       28.25000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.98500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.33000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.98500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.25000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.33000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P                                  
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     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 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     PRO A 617    O                                                   
REMARK 470     ASP P   1    CG   OD1  OD2                                       
REMARK 470     PRO P   7    CA   C    O    CB   CG   CD                         
REMARK 470     ARG P   2    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE P   8    CA   C    O    CB   CG   CD1  CD2  CE1  CE2  CZ     
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A    72     C2   NAG A  1630              2.05            
REMARK 500   NH1  ARG A   348     C8   NAG A  1630              1.47            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  72       79.26   -176.76                                   
REMARK 500    GLU A 123     -130.93     53.16                                   
REMARK 500    ALA A 296       76.22   -116.81                                   
REMARK 500    TYR P   4     -139.58   -102.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PE4 A 1629                                                       
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 A1627  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE P   5   O                                                      
REMARK 620 2 HIS A 383   NE2 110.5                                              
REMARK 620 3 GLU A 411   OE1  96.8 103.1                                        
REMARK 620 4 HIS A 387   NE2 120.4 116.7 105.5                                  
REMARK 620 5 TYR P   4   O    37.8  96.8 134.6 101.1                            
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  CL A1626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A1629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1634                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1635                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1636                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1637                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1638                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1630 BOUND TO ASN A  72                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 109 RESIDUES 1631 TO 1633                                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1O86   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERING ENZYME             
REMARK 900  IN COMPLEX WITH LISINOPRIL.                                         
REMARK 900 RELATED ID: 1O8A   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERING ENZYME (           
REMARK 900  NATIVE).                                                            
REMARK 900 RELATED ID: 1UZE   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF THE ANTI-HYPERTENSIVE DRUG ENALAPRIL AN THE              
REMARK 900   HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME                   
REMARK 900 RELATED ID: 1UZF   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF THE ANTI-HYPERTENSIVE DRUG CAPTOPRIL AN THE              
REMARK 900   HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME                   
REMARK 900 RELATED ID: 2C6F   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING                
REMARK 900  ENZYME N DOMAIN                                                     
REMARK 900 RELATED ID: 2C6N   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING                
REMARK 900  ENZYME N DOMAIN WITH LISINOPRIL                                     
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: 2WXW   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSINOGEN                          
REMARK 900 RELATED ID: 2X0B   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSINOGEN COMPLEXED WITH           
REMARK 900   RENIN                                                              
REMARK 900 RELATED ID: 2XY9   RELATED DB: PDB                                   
REMARK 900  HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH                 
REMARK 900  PHOSPHINIC TRIPEPTIDE                                               
REMARK 900 RELATED ID: 2XYD   RELATED DB: PDB                                   
REMARK 900  HUMAN ANGIOTENISN CONVERTING ENZYME N-DOMAIN IN COMPLEX             
REMARK 900   WITH PHOSPHINIC TRIPEPTIDE                                         
REMARK 900 RELATED ID: 2YDM   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL CHARACTERIZATION OF ANGIOTENSIN-I CONVERTING             
REMARK 900  ENZYME IN COMPLEX WITH A SELENIUM ANALOGUE OF                       
REMARK 900  CAPTOPRIL                                                           
REMARK 900 RELATED ID: 4AA1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE IN COMPLEX WITH ANGIOTENSIN-              
REMARK 900  II                                                                  
REMARK 900 RELATED ID: 4APJ   RELATED DB: PDB                                   
REMARK 900  HUMAN ANGIOTENSIN-CONVERTING ENZYME IN COMPLEX WITH BPPB            
DBREF  4APH A   37   625  UNP    P12821   ACE_HUMAN       68    656             
DBREF  4APH P    1     8  UNP    P01019   ANGT_HUMAN      34     41             
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                                              
SEQRES   1 P    8  ASP ARG VAL TYR ILE HIS PRO PHE                              
HET     CL  A1626       1                                                       
HET     ZN  A1627       1                                                       
HET     CL  A1628       1                                                       
HET    PE4  A1629      16                                                       
HET    NAG  A1630      14                                                       
HET    NAG  A1631      14                                                       
HET    NAG  A1632      14                                                       
HET    BMA  A1633      11                                                       
HET    ACT  A1634       4                                                       
HET    ACT  A1635       4                                                       
HET    ACT  A1636       4                                                       
HET    ACT  A1637       4                                                       
HET    ACT  A1638       4                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-                      
HETNAM   2 PE4  ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     ACT ACETATE ION                                                      
HETSYN     PE4 POLYETHYLENE GLYCOL PEG4000                                      
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5  PE4    C16 H34 O8                                                   
FORMUL   6  NAG    3(C8 H15 N O6)                                               
FORMUL   7  BMA    C6 H12 O6                                                    
FORMUL   8  ACT    5(C2 H3 O2 1-)                                               
FORMUL   9  HOH   *285(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  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  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  SER A  222  1                                   8    
HELIX   12  12 MET A  223  GLU A  225  5                                   3    
HELIX   13  13 SER A  228  LEU A  240  1                                  13    
HELIX   14  14 LEU A  240  GLY A  260  1                                  21    
HELIX   15  15 TRP A  283  ASN A  285  5                                   3    
HELIX   16  16 ILE A  286  VAL A  291  1                                   6    
HELIX   17  17 ASP A  300  GLN A  308  1                                   9    
HELIX   18  18 THR A  311  LEU A  326  1                                  16    
HELIX   19  19 PRO A  332  SER A  339  1                                   8    
HELIX   20  20 ASN A  374  TYR A  394  1                                  21    
HELIX   21  21 PRO A  398  ARG A  402  5                                   5    
HELIX   22  22 ASN A  406  SER A  422  1                                  17    
HELIX   23  23 THR A  423  LEU A  430  1                                   8    
HELIX   24  24 SER A  439  ASP A  473  1                                  35    
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  GLY A  611  1                                  23    
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 3 PHE A 365  LYS A 368  0                                        
SHEET    2  AC 3 SER A 355  ASP A 358 -1  O  SER A 355   N  LYS A 368           
SHEET    3  AC 3 ARG P   2  VAL P   3 -1  O  VAL P   3   N  ALA A 356           
SSBOND   1 CYS A  152    CYS A  158                          1555   1555  2.04  
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.05  
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.03  
LINK         ND2 ASN A  72                 C1  NAG A1630     1555   1555  1.43  
LINK         ND2 ASN A 109                 C1  NAG A1631     1555   1555  1.44  
LINK         NH1 ARG A 348                 C8  NAG A1630     1555   1555  1.47  
LINK        ZN    ZN A1627                 NE2 HIS A 387     1555   1555  2.06  
LINK        ZN    ZN A1627                 O  ATYR P   4     1555   1555  1.91  
LINK        ZN    ZN A1627                 O  BILE P   5     1555   1555  2.19  
LINK        ZN    ZN A1627                 NE2 HIS A 383     1555   1555  1.95  
LINK        ZN    ZN A1627                 OE1 GLU A 411     1555   1555  1.97  
LINK         O4  NAG A1631                 C1  NAG A1632     1555   1555  1.44  
LINK         O4  NAG A1632                 C1  BMA A1633     1555   1555  1.45  
CISPEP   1 GLU A  162    PRO A  163          0         1.71                     
SITE     1 AC1  4 TYR A 224  PRO A 519  ARG A 522  HOH A2112                    
SITE     1 AC2  5 HIS A 383  HIS A 387  GLU A 411  TYR P   4                    
SITE     2 AC2  5 ILE P   5                                                     
SITE     1 AC3  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 AC4  6 SER A 284  TYR A 287  LEU A 375  LYS A 449                    
SITE     2 AC4  6 ACT A1638  HOH A2172                                          
SITE     1 AC5  8 HIS A 383  GLU A 411  ASP A 415  TYR A 523                    
SITE     2 AC5  8 SER A 526  PHE A 527  HIS P   6  PRO P   7                    
SITE     1 AC6  8 TYR A 146  LEU A 161  TRP A 279  HIS A 353                    
SITE     2 AC6  8 LYS A 511  PHE A 512  HOH A2070  HOH A2163                    
SITE     1 AC7  2 ASP A 177  TRP A 180                                          
SITE     1 AC8  2 ASN A  85  ARG A 124                                          
SITE     1 AC9  5 TYR A 287  HIS A 442  ASN A 445  PHE A 446                    
SITE     2 AC9  5 PE4 A1629                                                     
SITE     1 BC1  2 ASN A  72  ARG A 348                                          
SITE     1 BC2  4 GLU A  43  ASN A 109  PRO A 398  HOH A2285                    
CRYST1   56.500   84.660  133.970  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      0.017699  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011812  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007464        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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