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Database: PDB
Entry: 2X92
LinkDB: 2X92
Original site: 2X92 
HEADER    HYDROLASE                               14-MAR-10   2X92              
TITLE     CRYSTAL STRUCTURE OF ANCE-RAMIPRILAT COMPLEX                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 17-615;                                           
COMPND   5 SYNONYM: DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II;                 
COMPND   6 EC: 3.4.15.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 644223;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: GS115;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPIC9                                     
KEYWDS    METALLOPROTEASE, CARBOXYPEPTIDASE, ACE INHIBITOR, HYDROLASE,          
KEYWDS   2 GLYCOPROTEIN                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.AKIF,D.GEORGIADIS,A.MAHAJAN,V.DIVE,E.D.STURROCK,R.E.ISAAC,          
AUTHOR   2 K.R.ACHARYA                                                          
REVDAT   4   12-JUL-17 2X92    1                                                
REVDAT   3   16-MAR-11 2X92    1       REMARK                                   
REVDAT   2   21-JUL-10 2X92    1       JRNL   ATOM                              
REVDAT   1   02-JUN-10 2X92    0                                                
JRNL        AUTH   M.AKIF,D.GEORGIADIS,A.MAHAJAN,V.DIVE,E.D.STURROCK,R.E.ISAAC, 
JRNL        AUTH 2 K.R.ACHARYA                                                  
JRNL        TITL   HIGH RESOLUTION CRYSTAL STRUCTURES OF DROSOPHILA             
JRNL        TITL 2 MELANOGASTER ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH   
JRNL        TITL 3 NOVEL INHIBITORS AND ANTI- HYPERTENSIVE DRUGS.               
JRNL        REF    J.MOL.BIOL.                   V. 400   502 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20488190                                                     
JRNL        DOI    10.1016/J.JMB.2010.05.024                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.11 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) : 2.11                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 59965                          
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3190                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.11                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3747                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 209                          
REMARK   3   BIN FREE R VALUE                    : 0.2570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4873                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 144                                     
REMARK   3   SOLVENT ATOMS            : 401                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.157         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.144         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.096         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.635         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5176 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7030 ; 1.002 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   601 ; 4.727 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   263 ;34.688 ;24.677       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   859 ;12.554 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;16.433 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   756 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3948 ; 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):  2999 ; 0.353 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4833 ; 0.732 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2177 ; 1.166 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2195 ; 2.003 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2X92 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290043251.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
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 CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66944                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.110                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       86.58450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.98958            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       34.53367            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       86.58450            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       49.98958            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       34.53367            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       86.58450            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       49.98958            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       34.53367            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       99.97917            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       69.06733            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       99.97917            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       69.06733            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       99.97917            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       69.06733            
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   615                                                      
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     LYS A  20    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
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  53       82.59   -162.70                                   
REMARK 500    ASP A 210      109.07   -162.20                                   
REMARK 500    LEU A 345     -129.17   -108.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1199        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A1200        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A1201        DISTANCE =  6.13 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 367   NE2                                                    
REMARK 620 2 HIS A 371   NE2 104.7                                              
REMARK 620 3 GLU A 395   OE1  96.4 110.3                                        
REMARK 620 4 X92 A 711   OAE 112.2 130.4  97.6                                  
REMARK 620 5 X92 A 711   OAB  92.1  92.5 152.6  55.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE ENZYME INHIBITOR                         
REMARK 630 MOLECULE NAME: RAMIPRILAT                                            
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     X92 A   711                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    CLT ALA XBG                                              
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 EPE A 1241                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  196 RESIDUES 1616 TO 1624                                           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1J38   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE G2P (LARGE TERMINASE) NUCLEASE DOMAIN FROM  
REMARK 900 THE BACTERIOPHAGE SPP1 WITH BOUND MN                                 
REMARK 900 RELATED ID: 1J36   RELATED DB: PDB                                   
REMARK 900 ISOMETRICALLY CONTRACTING INSECT ASYNCHRONOUS FLIGHT MUSCLE          
REMARK 900 RELATED ID: 1J37   RELATED DB: PDB                                   
REMARK 900 E. COLI COPPER AMINE OXIDASE IN COMPLEX WITH XENON                   
REMARK 900 RELATED ID: 2X94   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ANCE-PERINDOPRILAT COMPLEX                      
REMARK 900 RELATED ID: 2X8Z   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ANCE-CAPTOPRIL COMPLEX                          
REMARK 900 RELATED ID: 2X8Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ANCE                                            
REMARK 900 RELATED ID: 2X91   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ANCE-LISINOPRIL COMPLEX                         
REMARK 900 RELATED ID: 2X95   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ANCE-LISINOPRIL- TRYPTOPHAN ANALOGUE, LISW-S    
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 2X96   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ANCE-RXPA380 COMPLEX                            
REMARK 900 RELATED ID: 2X93   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ANCE-TRANDOLAPRILAT COMPLEX                     
REMARK 900 RELATED ID: 2X97   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ANCE-RXP407 COMPLEX                             
REMARK 900 RELATED ID: 2X90   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ANCE-ENALAPRILAT COMPLEX                        
DBREF  2X92 A   17   615  UNP    Q10714   ACE_DROME       17    615             
SEQRES   1 A  599  ALA LEU VAL LYS GLU GLU ILE GLN ALA LYS GLU TYR LEU          
SEQRES   2 A  599  GLU ASN LEU ASN LYS GLU LEU ALA LYS ARG THR ASN VAL          
SEQRES   3 A  599  GLU THR GLU ALA ALA TRP ALA TYR GLY SER ASN ILE THR          
SEQRES   4 A  599  ASP GLU ASN GLU LYS LYS LYS ASN GLU ILE SER ALA GLU          
SEQRES   5 A  599  LEU ALA LYS PHE MET LYS GLU VAL ALA SER ASP THR THR          
SEQRES   6 A  599  LYS PHE GLN TRP ARG SER TYR GLN SER GLU ASP LEU LYS          
SEQRES   7 A  599  ARG GLN PHE LYS ALA LEU THR LYS LEU GLY TYR ALA ALA          
SEQRES   8 A  599  LEU PRO GLU ASP ASP TYR ALA GLU LEU LEU ASP THR LEU          
SEQRES   9 A  599  SER ALA MET GLU SER ASN PHE ALA LYS VAL LYS VAL CYS          
SEQRES  10 A  599  ASP TYR LYS ASP SER THR LYS CYS ASP LEU ALA LEU ASP          
SEQRES  11 A  599  PRO GLU ILE GLU GLU VAL ILE SER LYS SER ARG ASP HIS          
SEQRES  12 A  599  GLU GLU LEU ALA TYR TYR TRP ARG GLU PHE TYR ASP LYS          
SEQRES  13 A  599  ALA GLY THR ALA VAL ARG SER GLN PHE GLU ARG TYR VAL          
SEQRES  14 A  599  GLU LEU ASN THR LYS ALA ALA LYS LEU ASN ASN PHE THR          
SEQRES  15 A  599  SER GLY ALA GLU ALA TRP LEU ASP GLU TYR GLU ASP ASP          
SEQRES  16 A  599  THR PHE GLU GLN GLN LEU GLU ASP ILE PHE ALA ASP ILE          
SEQRES  17 A  599  ARG PRO LEU TYR GLN GLN ILE HIS GLY TYR VAL ARG PHE          
SEQRES  18 A  599  ARG LEU ARG LYS HIS TYR GLY ASP ALA VAL VAL SER GLU          
SEQRES  19 A  599  THR GLY PRO ILE PRO MET HIS LEU LEU GLY ASN MET TRP          
SEQRES  20 A  599  ALA GLN GLN TRP SER GLU ILE ALA ASP ILE VAL SER PRO          
SEQRES  21 A  599  PHE PRO GLU LYS PRO LEU VAL ASP VAL SER ALA GLU MET          
SEQRES  22 A  599  GLU LYS GLN GLY TYR THR PRO LEU LYS MET PHE GLN MET          
SEQRES  23 A  599  GLY ASP ASP PHE PHE THR SER MET ASN LEU THR LYS LEU          
SEQRES  24 A  599  PRO GLN ASP PHE TRP ASP LYS SER ILE ILE GLU LYS PRO          
SEQRES  25 A  599  THR ASP GLY ARG ASP LEU VAL CYS HIS ALA SER ALA TRP          
SEQRES  26 A  599  ASP PHE TYR LEU THR ASP ASP VAL ARG ILE LYS GLN CYS          
SEQRES  27 A  599  THR ARG VAL THR GLN ASP GLN LEU PHE THR VAL HIS HIS          
SEQRES  28 A  599  GLU LEU GLY HIS ILE GLN TYR PHE LEU GLN TYR GLN HIS          
SEQRES  29 A  599  GLN PRO PHE VAL TYR ARG THR GLY ALA ASN PRO GLY PHE          
SEQRES  30 A  599  HIS GLU ALA VAL GLY ASP VAL LEU SER LEU SER VAL SER          
SEQRES  31 A  599  THR PRO LYS HIS LEU GLU LYS ILE GLY LEU LEU LYS ASP          
SEQRES  32 A  599  TYR VAL ARG ASP ASP GLU ALA ARG ILE ASN GLN LEU PHE          
SEQRES  33 A  599  LEU THR ALA LEU ASP LYS ILE VAL PHE LEU PRO PHE ALA          
SEQRES  34 A  599  PHE THR MET ASP LYS TYR ARG TRP SER LEU PHE ARG GLY          
SEQRES  35 A  599  GLU VAL ASP LYS ALA ASN TRP ASN CYS ALA PHE TRP LYS          
SEQRES  36 A  599  LEU ARG ASP GLU TYR SER GLY ILE GLU PRO PRO VAL VAL          
SEQRES  37 A  599  ARG SER GLU LYS ASP PHE ASP ALA PRO ALA LYS TYR HIS          
SEQRES  38 A  599  ILE SER ALA ASP VAL GLU TYR LEU ARG TYR LEU VAL SER          
SEQRES  39 A  599  PHE ILE ILE GLN PHE GLN PHE TYR LYS SER ALA CYS ILE          
SEQRES  40 A  599  LYS ALA GLY GLN TYR ASP PRO ASP ASN VAL GLU LEU PRO          
SEQRES  41 A  599  LEU ASP ASN CYS ASP ILE TYR GLY SER ALA ALA ALA GLY          
SEQRES  42 A  599  ALA ALA PHE HIS ASN MET LEU SER MET GLY ALA SER LYS          
SEQRES  43 A  599  PRO TRP PRO ASP ALA LEU GLU ALA PHE ASN GLY GLU ARG          
SEQRES  44 A  599  ILE MET SER GLY LYS ALA ILE ALA GLU TYR PHE GLU PRO          
SEQRES  45 A  599  LEU ARG VAL TRP LEU GLU ALA GLU ASN ILE LYS ASN ASN          
SEQRES  46 A  599  VAL HIS ILE GLY TRP THR THR SER ASN LYS CYS VAL SER          
SEQRES  47 A  599  SER                                                          
MODRES 2X92 ASN A   53  ASN  GLYCOSYLATION SITE                                 
MODRES 2X92 ASN A  196  ASN  GLYCOSYLATION SITE                                 
MODRES 2X92 ASN A  311  ASN  GLYCOSYLATION SITE                                 
HET    EPE  A 701      15                                                       
HET     ZN  A 702       1                                                       
HET    NAG  A 703      14                                                       
HET    NAG  A 704      14                                                       
HET    BMA  A 705      11                                                       
HET    BMA  A 706      11                                                       
HET    MAN  A 707      11                                                       
HET    MAN  A 708      11                                                       
HET    NAG  A 709      14                                                       
HET    NAG  A 710      14                                                       
HET    X92  A 711      28                                                       
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM      ZN ZINC ION                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     X92 RAMIPRILAT                                                       
HETSYN     EPE HEPES                                                            
FORMUL   2  EPE    C8 H18 N2 O4 S                                               
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  NAG    4(C8 H15 N O6)                                               
FORMUL   4  BMA    2(C6 H12 O6)                                                 
FORMUL   4  MAN    2(C6 H12 O6)                                                 
FORMUL   7  X92    C21 H28 N2 O5                                                
FORMUL   8  HOH   *401(H2 O)                                                    
HELIX    1   1 ALA A   17  ASN A   53  1                                  37    
HELIX    2   2 THR A   55  THR A   80  1                                  26    
HELIX    3   3 THR A   81  PHE A   83  5                                   3    
HELIX    4   4 GLN A   84  TYR A   88  5                                   5    
HELIX    5   5 SER A   90  LEU A  100  1                                  11    
HELIX    6   6 LEU A  103  LEU A  108  5                                   6    
HELIX    7   7 PRO A  109  LYS A  129  1                                  21    
HELIX    8   8 PRO A  147  SER A  156  1                                  10    
HELIX    9   9 ASP A  158  GLY A  174  1                                  17    
HELIX   10  10 VAL A  177  ASN A  195  1                                  19    
HELIX   11  11 SER A  199  GLU A  207  1                                   9    
HELIX   12  12 THR A  212  GLY A  244  1                                  33    
HELIX   13  13 HIS A  257  LEU A  259  5                                   3    
HELIX   14  14 TRP A  267  GLU A  269  5                                   3    
HELIX   15  15 ILE A  270  SER A  275  1                                   6    
HELIX   16  16 VAL A  285  GLN A  292  1                                   8    
HELIX   17  17 THR A  295  MET A  310  1                                  16    
HELIX   18  18 PRO A  316  SER A  323  1                                   8    
HELIX   19  19 THR A  358  TYR A  378  1                                  21    
HELIX   20  20 PRO A  382  ARG A  386  5                                   5    
HELIX   21  21 ASN A  390  SER A  406  1                                  17    
HELIX   22  22 THR A  407  ILE A  414  1                                   8    
HELIX   23  23 ASP A  423  ILE A  439  1                                  17    
HELIX   24  24 VAL A  440  ARG A  457  1                                  18    
HELIX   25  25 ASP A  461  ALA A  463  5                                   3    
HELIX   26  26 ASN A  464  GLY A  478  1                                  15    
HELIX   27  27 ASP A  491  ALA A  494  5                                   4    
HELIX   28  28 LYS A  495  ALA A  500  1                                   6    
HELIX   29  29 TYR A  504  ALA A  525  1                                  22    
HELIX   30  30 PRO A  536  CYS A  540  5                                   5    
HELIX   31  31 SER A  545  SER A  557  1                                  13    
HELIX   32  32 PRO A  563  GLY A  573  1                                  11    
HELIX   33  33 GLY A  579  ASN A  600  1                                  22    
SHEET    1  AA 2 ILE A 254  PRO A 255  0                                        
SHEET    2  AA 2 ILE A 479  GLU A 480  1  N  GLU A 480   O  ILE A 254           
SHEET    1  AB 2 SER A 339  ASP A 342  0                                        
SHEET    2  AB 2 VAL A 349  LYS A 352 -1  O  ARG A 350   N  TRP A 341           
SHEET    1  AC 2 ARG A 485  SER A 486  0                                        
SHEET    2  AC 2 CYS A 612  VAL A 613  1  N  VAL A 613   O  ARG A 485           
SSBOND   1 CYS A  133    CYS A  141                          1555   1555  2.05  
SSBOND   2 CYS A  336    CYS A  354                          1555   1555  2.05  
SSBOND   3 CYS A  467    CYS A  612                          1555   1555  2.07  
SSBOND   4 CYS A  522    CYS A  540                          1555   1555  2.03  
LINK         ND2 ASN A  53                 C1  NAG A 710     1555   1555  1.46  
LINK         ND2 ASN A 196                 C1  NAG A 703     1555   1555  1.44  
LINK         ND2 ASN A 311                 C1  NAG A 709     1555   1555  1.44  
LINK         NE2 HIS A 367                ZN    ZN A 702     1555   1555  2.04  
LINK         NE2 HIS A 371                ZN    ZN A 702     1555   1555  2.01  
LINK         OE1 GLU A 395                ZN    ZN A 702     1555   1555  1.95  
LINK        ZN    ZN A 702                 OAE X92 A 711     1555   1555  2.29  
LINK        ZN    ZN A 702                 OAB X92 A 711     1555   1555  2.45  
LINK         O4  NAG A 703                 C1  NAG A 704     1555   1555  1.44  
LINK         O4  NAG A 704                 C1  BMA A 705     1555   1555  1.45  
LINK         O3  BMA A 705                 C1  MAN A 708     1555   1555  1.44  
LINK         O6  BMA A 705                 C1  MAN A 707     1555   1555  1.44  
LINK         C1  BMA A 706                 O6  MAN A 708     1555   1555  1.45  
CISPEP   1 ASP A  146    PRO A  147          0         3.72                     
SITE     1 AC1  6 ALA A 340  TRP A 341  HIS A 394  X92 A 711                    
SITE     2 AC1  6 HOH A 948  HOH A1060                                          
SITE     1 AC2  4 HIS A 367  HIS A 371  GLU A 395  X92 A 711                    
SITE     1 AC3 31 ASN A  53  THR A  55  GLU A  57  GLN A  84                    
SITE     2 AC3 31 ASN A 196  GLN A 265  ASN A 311  ASP A 330                    
SITE     3 AC3 31 ARG A 332  HIS A 337  ALA A 338  HIS A 367                    
SITE     4 AC3 31 GLU A 368  HIS A 371  GLU A 395  LYS A 495                    
SITE     5 AC3 31 TYR A 496  HIS A 497  VAL A 502  TYR A 504                    
SITE     6 AC3 31 TYR A 507  EPE A 701   ZN A 702  HOH A 828                    
SITE     7 AC3 31 HOH A1040  HOH A1041  HOH A 963  HOH A 971                    
SITE     8 AC3 31 HOH A 845  HOH A1068  HOH A 877                               
CRYST1  173.169  173.169  103.601  90.00  90.00 120.00 H 3           9          
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      0.005775  0.003334  0.000000        0.00000                         
SCALE2      0.000000  0.006668  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009652        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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