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Database: PDB
Entry: 4ASQ
LinkDB: 4ASQ
Original site: 4ASQ 
HEADER    HYDROLASE                               02-MAY-12   4ASQ              
TITLE     CRYSTAL STRUCTURE OF ANCE IN COMPLEX WITH BRADYKININ                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 17-614;                                           
COMPND   5 SYNONYM: DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II;                 
COMPND   6 EC: 3.4.15.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: BRADYKININ;                                                
COMPND  10 CHAIN: P                                                             
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: KOMAGATAELLA 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;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    HYDROLASE, ZINC METALLOPROTEASE, SUBSTRATE RECOGNITION                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.AKIF,G.MASUYER,E.D.STURROCK,R.E.ISAAC,K.R.ACHARYA                   
REVDAT   3   19-DEC-12 4ASQ    1       JRNL                                     
REVDAT   2   05-DEC-12 4ASQ    1       JRNL                                     
REVDAT   1   31-OCT-12 4ASQ    0                                                
JRNL        AUTH   M.AKIF,G.MASUYER,R.J.BINGHAM,E.D.STURROCK,R.E.ISAAC,         
JRNL        AUTH 2 K.R.ACHARYA                                                  
JRNL        TITL   STRUCTURAL BASIS OF PEPTIDE RECOGNITION BY THE               
JRNL        TITL 2 ANGIOTENSIN-I CONVERTING ENZYME HOMOLOGUE ANCE FROM          
JRNL        TITL 3 DROSOPHILA MELANOGASTER                                      
JRNL        REF    FEBS J.                       V. 279  4525 2012              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   23082758                                                     
JRNL        DOI    10.1111/FEBS.12038                                           
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) : 86.56                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.41                          
REMARK   3   NUMBER OF REFLECTIONS             : 72831                          
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) : 0.18132                         
REMARK   3   R VALUE            (WORKING SET) : 0.18035                         
REMARK   3   FREE R VALUE                     : 0.19987                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3847                            
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) : 5379                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.51                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.226                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 258                          
REMARK   3   BIN FREE R VALUE                    : 0.262                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4924                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 114                                     
REMARK   3   SOLVENT ATOMS            : 500                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.318                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.43                                                
REMARK   3    B22 (A**2) : -2.43                                                
REMARK   3    B33 (A**2) : 3.65                                                 
REMARK   3    B12 (A**2) : -1.22                                                
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): 0.121         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.112         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.077         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.865         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5178 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7034 ; 0.914 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   605 ; 4.618 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   264 ;34.289 ;24.621       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   864 ;12.022 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;15.816 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   756 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3972 ; 0.003 ; 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):  3018 ; 0.223 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4867 ; 0.454 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2160 ; 0.760 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2165 ; 1.335 ; 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 : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    17        A   614                          
REMARK   3    RESIDUE RANGE :   P     1        A     3                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8157  25.6732 -12.8928              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0612 T22:   0.0522                                     
REMARK   3      T33:   0.0719 T12:   0.0156                                     
REMARK   3      T13:   0.0124 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6095 L22:   0.2607                                     
REMARK   3      L33:   0.2500 L12:   0.0470                                     
REMARK   3      L13:  -0.2495 L23:  -0.1124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0831 S12:  -0.0428 S13:  -0.1256                       
REMARK   3      S21:  -0.0166 S22:  -0.0413 S23:  -0.0521                       
REMARK   3      S31:  -0.0089 S32:   0.0000 S33:   0.1244                       
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. ONLY RESIDUES 1-3 OF BRADYKININ ARE              
REMARK   3   VISIBLE                                                            
REMARK   4                                                                      
REMARK   4 4ASQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAY-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-52366.                                       
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        : 1                                  
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 (Q315)                         
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : TRUNCATE                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89919                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.97                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 2.3                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.20                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.42                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2X8Y                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES 1.3 M SODIUM                
REMARK 280  CITRATE                                                             
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       86.56250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.97688            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       33.89100            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       86.56250            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       49.97688            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       33.89100            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       86.56250            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       49.97688            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       33.89100            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       99.95377            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       67.78200            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       99.95377            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       67.78200            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       99.95377            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       67.78200            
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: 2810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.9 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     PHE P     5                                                      
REMARK 465     SER P     6                                                      
REMARK 465     PRO P     7                                                      
REMARK 465     PHE P     8                                                      
REMARK 465     ARG P     9                                                      
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     GLY P   4    CA   C    O                                         
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    53     C1   NAG A  1623              1.44            
REMARK 500   ND2  ASN A   311     C1   NAG A  1622              1.44            
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  53       85.14   -159.96                                   
REMARK 500    LEU A 345     -132.96   -105.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1615  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 371   NE2                                                    
REMARK 620 2 HIS A 367   NE2 102.6                                              
REMARK 620 3 ARG P   1   O   170.9  82.7                                        
REMARK 620 4 GLU A 395   OE1 101.5  94.4  85.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A1624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 196 RESIDUES 1616 TO 1621                                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1J36   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF DROSOPHILA ANCE                                
REMARK 900 RELATED ID: 1J37   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF DROSOPHILA ANCE                                
REMARK 900 RELATED ID: 1J38   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF DROSOPHILA ANCE                                
REMARK 900 RELATED ID: 2X8Y   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE                                           
REMARK 900 RELATED ID: 2X8Z   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-CAPTOPRIL COMPLEX                         
REMARK 900 RELATED ID: 2X90   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-ENALAPRILAT COMPLEX                       
REMARK 900 RELATED ID: 2X91   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-LISINOPRIL COMPLEX                        
REMARK 900 RELATED ID: 2X92   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-RAMIPRILAT COMPLEX                        
REMARK 900 RELATED ID: 2X93   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-TRANDOLAPRILAT COMPLEX                    
REMARK 900 RELATED ID: 2X94   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-PERINDOPRILAT COMPLEX                     
REMARK 900 RELATED ID: 2X95   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-LISINOPRIL-TRYPTOPHAN ANALOGUE            
REMARK 900  , LISW-S COMPLEX                                                    
REMARK 900 RELATED ID: 2X96   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-RXPA380 COMPLEX                           
REMARK 900 RELATED ID: 2X97   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-RXP407 COMPLEX                            
REMARK 900 RELATED ID: 2XHM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-K26 COMPLEX                               
REMARK 900 RELATED ID: 3ZQZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE IN COMPLEX WITH A SELENIUM                
REMARK 900  ANALOGUE OF 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: 4AA2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE IN COMPLEX WITH BRADYKININ                
REMARK 900  POTENTIATING PEPTIDE B                                              
REMARK 900 RELATED ID: 4ASR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE IN COMPLEX WITH THR6-                     
REMARK 900  BRADYKININ                                                          
DBREF  4ASQ A   17   614  UNP    Q10714   ACE_DROME       17    614             
DBREF  4ASQ P    1     9  UNP    P01042   KNG1_HUMA      381    389             
SEQRES   1 A  598  ALA LEU VAL LYS GLU GLU ILE GLN ALA LYS GLU TYR LEU          
SEQRES   2 A  598  GLU ASN LEU ASN LYS GLU LEU ALA LYS ARG THR ASN VAL          
SEQRES   3 A  598  GLU THR GLU ALA ALA TRP ALA TYR GLY SER ASN ILE THR          
SEQRES   4 A  598  ASP GLU ASN GLU LYS LYS LYS ASN GLU ILE SER ALA GLU          
SEQRES   5 A  598  LEU ALA LYS PHE MET LYS GLU VAL ALA SER ASP THR THR          
SEQRES   6 A  598  LYS PHE GLN TRP ARG SER TYR GLN SER GLU ASP LEU LYS          
SEQRES   7 A  598  ARG GLN PHE LYS ALA LEU THR LYS LEU GLY TYR ALA ALA          
SEQRES   8 A  598  LEU PRO GLU ASP ASP TYR ALA GLU LEU LEU ASP THR LEU          
SEQRES   9 A  598  SER ALA MET GLU SER ASN PHE ALA LYS VAL LYS VAL CYS          
SEQRES  10 A  598  ASP TYR LYS ASP SER THR LYS CYS ASP LEU ALA LEU ASP          
SEQRES  11 A  598  PRO GLU ILE GLU GLU VAL ILE SER LYS SER ARG ASP HIS          
SEQRES  12 A  598  GLU GLU LEU ALA TYR TYR TRP ARG GLU PHE TYR ASP LYS          
SEQRES  13 A  598  ALA GLY THR ALA VAL ARG SER GLN PHE GLU ARG TYR VAL          
SEQRES  14 A  598  GLU LEU ASN THR LYS ALA ALA LYS LEU ASN ASN PHE THR          
SEQRES  15 A  598  SER GLY ALA GLU ALA TRP LEU ASP GLU TYR GLU ASP ASP          
SEQRES  16 A  598  THR PHE GLU GLN GLN LEU GLU ASP ILE PHE ALA ASP ILE          
SEQRES  17 A  598  ARG PRO LEU TYR GLN GLN ILE HIS GLY TYR VAL ARG PHE          
SEQRES  18 A  598  ARG LEU ARG LYS HIS TYR GLY ASP ALA VAL VAL SER GLU          
SEQRES  19 A  598  THR GLY PRO ILE PRO MET HIS LEU LEU GLY ASN MET TRP          
SEQRES  20 A  598  ALA GLN GLN TRP SER GLU ILE ALA ASP ILE VAL SER PRO          
SEQRES  21 A  598  PHE PRO GLU LYS PRO LEU VAL ASP VAL SER ALA GLU MET          
SEQRES  22 A  598  GLU LYS GLN GLY TYR THR PRO LEU LYS MET PHE GLN MET          
SEQRES  23 A  598  GLY ASP ASP PHE PHE THR SER MET ASN LEU THR LYS LEU          
SEQRES  24 A  598  PRO GLN ASP PHE TRP ASP LYS SER ILE ILE GLU LYS PRO          
SEQRES  25 A  598  THR ASP GLY ARG ASP LEU VAL CYS HIS ALA SER ALA TRP          
SEQRES  26 A  598  ASP PHE TYR LEU THR ASP ASP VAL ARG ILE LYS GLN CYS          
SEQRES  27 A  598  THR ARG VAL THR GLN ASP GLN LEU PHE THR VAL HIS HIS          
SEQRES  28 A  598  GLU LEU GLY HIS ILE GLN TYR PHE LEU GLN TYR GLN HIS          
SEQRES  29 A  598  GLN PRO PHE VAL TYR ARG THR GLY ALA ASN PRO GLY PHE          
SEQRES  30 A  598  HIS GLU ALA VAL GLY ASP VAL LEU SER LEU SER VAL SER          
SEQRES  31 A  598  THR PRO LYS HIS LEU GLU LYS ILE GLY LEU LEU LYS ASP          
SEQRES  32 A  598  TYR VAL ARG ASP ASP GLU ALA ARG ILE ASN GLN LEU PHE          
SEQRES  33 A  598  LEU THR ALA LEU ASP LYS ILE VAL PHE LEU PRO PHE ALA          
SEQRES  34 A  598  PHE THR MET ASP LYS TYR ARG TRP SER LEU PHE ARG GLY          
SEQRES  35 A  598  GLU VAL ASP LYS ALA ASN TRP ASN CYS ALA PHE TRP LYS          
SEQRES  36 A  598  LEU ARG ASP GLU TYR SER GLY ILE GLU PRO PRO VAL VAL          
SEQRES  37 A  598  ARG SER GLU LYS ASP PHE ASP ALA PRO ALA LYS TYR HIS          
SEQRES  38 A  598  ILE SER ALA ASP VAL GLU TYR LEU ARG TYR LEU VAL SER          
SEQRES  39 A  598  PHE ILE ILE GLN PHE GLN PHE TYR LYS SER ALA CYS ILE          
SEQRES  40 A  598  LYS ALA GLY GLN TYR ASP PRO ASP ASN VAL GLU LEU PRO          
SEQRES  41 A  598  LEU ASP ASN CYS ASP ILE TYR GLY SER ALA ALA ALA GLY          
SEQRES  42 A  598  ALA ALA PHE HIS ASN MET LEU SER MET GLY ALA SER LYS          
SEQRES  43 A  598  PRO TRP PRO ASP ALA LEU GLU ALA PHE ASN GLY GLU ARG          
SEQRES  44 A  598  ILE MET SER GLY LYS ALA ILE ALA GLU TYR PHE GLU PRO          
SEQRES  45 A  598  LEU ARG VAL TRP LEU GLU ALA GLU ASN ILE LYS ASN ASN          
SEQRES  46 A  598  VAL HIS ILE GLY TRP THR THR SER ASN LYS CYS VAL SER          
SEQRES   1 P    9  ARG PRO PRO GLY PHE SER PRO PHE ARG                          
HET     ZN  A1615       1                                                       
HET    NAG  A1616      14                                                       
HET    NAG  A1617      14                                                       
HET    MAN  A1618      11                                                       
HET    BMA  A1619      11                                                       
HET    BMA  A1620      11                                                       
HET    MAN  A1621      11                                                       
HET    NAG  A1622      14                                                       
HET    NAG  A1623      14                                                       
HET    FLC  A1624      13                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     FLC CITRATE ANION                                                    
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  NAG    4(C8 H15 N O6)                                               
FORMUL   5  MAN    2(C6 H12 O6)                                                 
FORMUL   6  BMA    2(C6 H12 O6)                                                 
FORMUL   7  FLC    C6 H5 O7 3-                                                  
FORMUL   8  HOH   *500(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  LYS A  102  1                                  13    
HELIX    6   6 LEU A  103  LEU A  108  5                                   6    
HELIX    7   7 PRO A  109  VAL A  130  1                                  22    
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  ASP A  206  1                                   8    
HELIX   12  12 GLU A  207  GLU A  209  5                                   3    
HELIX   13  13 THR A  212  GLY A  244  1                                  33    
HELIX   14  14 HIS A  257  LEU A  259  5                                   3    
HELIX   15  15 TRP A  267  GLU A  269  5                                   3    
HELIX   16  16 ILE A  270  SER A  275  1                                   6    
HELIX   17  17 VAL A  285  GLN A  292  1                                   8    
HELIX   18  18 THR A  295  MET A  310  1                                  16    
HELIX   19  19 PRO A  316  SER A  323  1                                   8    
HELIX   20  20 THR A  358  GLN A  379  1                                  22    
HELIX   21  21 PRO A  382  ARG A  386  5                                   5    
HELIX   22  22 ASN A  390  SER A  406  1                                  17    
HELIX   23  23 THR A  407  ILE A  414  1                                   8    
HELIX   24  24 ASP A  423  ILE A  439  1                                  17    
HELIX   25  25 VAL A  440  ARG A  457  1                                  18    
HELIX   26  26 ASP A  461  ALA A  463  5                                   3    
HELIX   27  27 ASN A  464  GLY A  478  1                                  15    
HELIX   28  28 ASP A  491  ALA A  494  5                                   4    
HELIX   29  29 LYS A  495  ALA A  500  1                                   6    
HELIX   30  30 TYR A  504  ALA A  525  1                                  22    
HELIX   31  31 PRO A  536  CYS A  540  5                                   5    
HELIX   32  32 SER A  545  SER A  557  1                                  13    
HELIX   33  33 PRO A  563  GLY A  573  1                                  11    
HELIX   34  34 GLY A  579  ASN A  600  1                                  22    
SHEET    1  AA 2 LYS A 131  VAL A 132  0                                        
SHEET    2  AA 2 LEU A 143  ALA A 144 -1  O  LEU A 143   N  VAL A 132           
SHEET    1  AB 2 ILE A 254  PRO A 255  0                                        
SHEET    2  AB 2 ILE A 479  GLU A 480  1  N  GLU A 480   O  ILE A 254           
SHEET    1  AC 2 SER A 339  ASP A 342  0                                        
SHEET    2  AC 2 VAL A 349  LYS A 352 -1  O  ARG A 350   N  TRP A 341           
SHEET    1  AD 2 ARG A 485  SER A 486  0                                        
SHEET    2  AD 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  2.04  
SSBOND   2 CYS A  336    CYS A  354                          1555   1555  2.04  
SSBOND   3 CYS A  467    CYS A  612                          1555   1555  2.05  
SSBOND   4 CYS A  522    CYS A  540                          1555   1555  2.03  
LINK         ND2 ASN A 196                 C1  NAG A1616     1555   1555  1.44  
LINK        ZN    ZN A1615                 NE2 HIS A 367     1555   1555  2.07  
LINK        ZN    ZN A1615                 O   ARG P   1     1555   1555  2.49  
LINK        ZN    ZN A1615                 OE1 GLU A 395     1555   1555  2.01  
LINK        ZN    ZN A1615                 NE2 HIS A 371     1555   1555  2.07  
LINK         O4  NAG A1616                 C1  NAG A1617     1555   1555  1.44  
LINK         O6  BMA A1619                 C1  MAN A1621     1555   1555  1.44  
LINK         O3  BMA A1619                 C1  MAN A1618     1555   1555  1.45  
LINK         C1  BMA A1619                 O4  NAG A1617     1555   1555  1.45  
LINK         C1  BMA A1620                 O6  MAN A1618     1555   1555  1.44  
CISPEP   1 ASP A  146    PRO A  147          0         4.89                     
SITE     1 AC1  4 HIS A 367  HIS A 371  GLU A 395  ARG P   1                    
SITE     1 AC2  1 ASN A 311                                                     
SITE     1 AC3  6 ASN A  53  THR A  55  GLU A  57  ASN A  58                    
SITE     2 AC3  6 ASP A 330  ARG A 332                                          
SITE     1 AC4  5 SER A 339  ALA A 340  GLU A 368  HIS A 371                    
SITE     2 AC4  5 ARG P   1                                                     
SITE     1 AC5 16 GLN A  84  ARG A 157  HIS A 159  ASN A 196                    
SITE     2 AC5 16 ARG A 238  LYS A 241  HIS A 242  TYR A 243                    
SITE     3 AC5 16 PRO A 278  HOH A2269  HOH A2271  HOH A2272                    
SITE     4 AC5 16 HOH A2297  HOH A2494  HOH A2495  HOH A2496                    
CRYST1  173.125  173.125  101.673  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      0.005776  0.003335  0.000000        0.00000                         
SCALE2      0.000000  0.006670  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009835        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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