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Database: PDB
Entry: 3ZQZ
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Original site: 3ZQZ 
HEADER    HYDROLASE                               13-JUN-11   3ZQZ              
TITLE     CRYSTAL STRUCTURE OF ANCE IN COMPLEX WITH A SELENIUM ANALOGUE OF      
TITLE    2 CAPTOPRIL                                                            
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, ANCE;           
COMPND   6 EC: 3.4.15.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_TAXID: 7227;                                                
SOURCE   4 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 644223;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: GS115;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PPIC9                                     
KEYWDS    HYDROLASE, INHIBITOR DESIGN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.AKIF,G.MASUYER,S.L.U.SCHWAGER,B.J.BHUYAN,G.MUGESH,R.E.ISAAC,        
AUTHOR   2 E.D.STURROCK,K.R.ACHARYA                                             
REVDAT   2   05-OCT-11 3ZQZ    1       JRNL                                     
REVDAT   1   14-SEP-11 3ZQZ    0                                                
JRNL        AUTH   M.AKIF,G.MASUYER,S.L.SCHWAGER,B.J.BHUYAN,G.MUGESH,R.E.ISAAC, 
JRNL        AUTH 2 E.D.STURROCK,K.R.ACHARYA                                     
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF ANGIOTENSIN I- CONVERTING     
JRNL        TITL 2 ENZYME IN COMPLEX WITH A SELENIUM ANALOGUE OF CAPTOPRIL.     
JRNL        REF    FEBS J.                       V. 278  3644 2011              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   21810173                                                     
JRNL        DOI    10.1111/J.1742-4658.2011.08276.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 86.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.84                          
REMARK   3   NUMBER OF REFLECTIONS             : 42393                          
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) : 0.20577                         
REMARK   3   R VALUE            (WORKING SET) : 0.20404                         
REMARK   3   FREE R VALUE                     : 0.23756                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2267                            
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) : 2.353                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.414                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2104                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.11                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.384                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 101                          
REMARK   3   BIN FREE R VALUE                    : 0.468                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4862                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 115                                     
REMARK   3   SOLVENT ATOMS            : 201                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.3                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.003                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.03                                                
REMARK   3    B22 (A**2) : -6.03                                                
REMARK   3    B33 (A**2) : 9.04                                                 
REMARK   3    B12 (A**2) : -3.01                                                
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): 0.243         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.202         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.204         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.972        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5117 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6950 ; 0.876 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   599 ; 5.862 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   261 ;37.132 ;24.713       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   847 ;15.937 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;14.875 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   747 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3926 ; 0.006 ; 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):  2986 ; 0.352 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4808 ; 0.693 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2131 ; 1.186 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2139 ; 1.939 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    19        A  1626                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.6352   3.0809 -12.3611              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1512 T22:   0.1580                                     
REMARK   3      T33:   0.1635 T12:  -0.0018                                     
REMARK   3      T13:  -0.0008 T23:  -0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5295 L22:   1.2603                                     
REMARK   3      L33:   0.3310 L12:   0.3146                                     
REMARK   3      L13:   0.1168 L23:   0.4759                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0557 S12:  -0.0297 S13:   0.1239                       
REMARK   3      S21:   0.0360 S22:  -0.1517 S23:   0.4359                       
REMARK   3      S31:   0.0152 S32:   0.0543 S33:   0.2074                       
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. U VALUES WITH TLS ADDED                          
REMARK   4                                                                      
REMARK   4 3ZQZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-48688.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAY-11                          
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                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (PILATUS 6M)                   
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44663                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.35                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.97                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 4.0                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.53                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.60                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2X8Z                                       
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): 4.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES 7.5, 1.3 M SODIUM 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       86.89850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       50.17087            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       33.59833            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       86.89850            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       50.17087            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       33.59833            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       86.89850            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       50.17087            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       33.59833            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      100.34174            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       67.19667            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      100.34174            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       67.19667            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      100.34174            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       67.19667            
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     ALA A    17                                                      
REMARK 465     LEU A    18                                                      
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     VAL A  19    CG1  CG2                                            
REMARK 470     LYS A  20    CG   CD   CE   NZ                                   
REMARK 470     GLN A  24    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 488    CD   CE   NZ                                        
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   196     O5   NAG A  1617              1.61            
REMARK 500   ND2  ASN A   311     C2   NAG A  1621              1.98            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2017     O    HOH A  2195     8544     2.17            
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       85.16   -161.72                                   
REMARK 500    ASP A 284       82.54   -153.12                                   
REMARK 500    LEU A 345     -133.65   -102.58                                   
REMARK 500    ASN A 572       13.24   -140.47                                   
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 A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 371   NE2                                                    
REMARK 620 2 HIS A 367   NE2  94.3                                              
REMARK 620 3 GLU A 395   OE1  87.5  85.4                                        
REMARK 620 4 SLC A1626  SE   124.5 114.1 138.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: SELENO-CAPTOPRIL                                      
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     SLC A  1626                                                      
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP: PRO CC4                                                     
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  ZN A1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SLC A1626                 
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 1617 TO 1624                                          
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2X94   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-PERINDOPRILAT COMPLEX                     
REMARK 900 RELATED ID: 1J38   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF DROSOPHILA ANCE                                
REMARK 900 RELATED ID: 2X8Z   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-CAPTOPRIL COMPLEX                         
REMARK 900 RELATED ID: 1J36   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF DROSOPHILA ANCE                                
REMARK 900 RELATED ID: 2XHM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-K26 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            
REMARK 900  , LISW-S COMPLEX                                                    
REMARK 900 RELATED ID: 2X92   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ANCE-RAMIPRILAT 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                       
REMARK 900 RELATED ID: 1J37   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF DROSOPHILA ANCE                                
DBREF  3ZQZ A   17   614  UNP    Q10714   ACE_DROME       17    614             
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          
HET     ZN  A1001       1                                                       
HET    NAG  A1617      14                                                       
HET    NAG  A1618      14                                                       
HET    BMA  A1619      11                                                       
HET    MAN  A1620      11                                                       
HET    NAG  A1621      14                                                       
HET    NAG  A1622      14                                                       
HET    MAN  A1623      11                                                       
HET    BMA  A1624      11                                                       
HET    SLC  A1626      14                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     SLC SELENO-CAPTOPRIL                                                 
HETSYN     SLC 1-[2-(SELANYLMETHYL)ACRYLOYL]-L-PROLINE                          
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   4  BMA    2(C6 H12 O6)                                                 
FORMUL   5  MAN    2(C6 H12 O6)                                                 
FORMUL   6  SLC    C9 H13 N O3 SE                                               
FORMUL   7  HOH   *201(H2 O)                                                    
HELIX    1   1 GLU A   21  ASN A   53  1                                  33    
HELIX    2   2 THR A   55  THR A   81  1                                  27    
HELIX    3   3 GLN A   84  TYR A   88  5                                   5    
HELIX    4   4 SER A   90  LYS A  102  1                                  13    
HELIX    5   5 LEU A  103  LEU A  108  5                                   6    
HELIX    6   6 PRO A  109  LYS A  129  1                                  21    
HELIX    7   7 PRO A  147  SER A  156  1                                  10    
HELIX    8   8 ASP A  158  GLY A  174  1                                  17    
HELIX    9   9 VAL A  177  ASN A  195  1                                  19    
HELIX   10  10 SER A  199  GLU A  207  1                                   9    
HELIX   11  11 THR A  212  GLY A  244  1                                  33    
HELIX   12  12 HIS A  257  LEU A  259  5                                   3    
HELIX   13  13 TRP A  267  GLU A  269  5                                   3    
HELIX   14  14 ILE A  270  SER A  275  1                                   6    
HELIX   15  15 VAL A  285  GLN A  292  1                                   8    
HELIX   16  16 THR A  295  MET A  310  1                                  16    
HELIX   17  17 PRO A  316  SER A  323  1                                   8    
HELIX   18  18 THR A  358  GLN A  379  1                                  22    
HELIX   19  19 PRO A  382  ARG A  386  5                                   5    
HELIX   20  20 ASN A  390  SER A  406  1                                  17    
HELIX   21  21 THR A  407  ILE A  414  1                                   8    
HELIX   22  22 ASP A  423  ILE A  439  1                                  17    
HELIX   23  23 VAL A  440  ARG A  457  1                                  18    
HELIX   24  24 ASP A  461  TRP A  465  5                                   5    
HELIX   25  25 ASN A  466  GLY A  478  1                                  13    
HELIX   26  26 ASP A  491  ALA A  494  5                                   4    
HELIX   27  27 LYS A  495  ALA A  500  1                                   6    
HELIX   28  28 TYR A  504  ALA A  525  1                                  22    
HELIX   29  29 PRO A  536  CYS A  540  5                                   5    
HELIX   30  30 SER A  545  SER A  557  1                                  13    
HELIX   31  31 PRO A  563  GLY A  573  1                                  11    
HELIX   32  32 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  2.04  
SSBOND   2 CYS A  336    CYS A  354                          1555   1555  2.06  
SSBOND   3 CYS A  467    CYS A  612                          1555   1555  2.06  
SSBOND   4 CYS A  522    CYS A  540                          1555   1555  2.02  
LINK         ND2 ASN A  53                 C1  NAG A1622     1555   1555  1.45  
LINK         ND2 ASN A 196                 C1  NAG A1617     1555   1555  1.29  
LINK         ND2 ASN A 311                 C1  NAG A1621     1555   1555  1.44  
LINK        ZN    ZN A1001                 NE2 HIS A 367     1555   1555  2.18  
LINK        ZN    ZN A1001                SE   SLC A1626     1555   1555  2.73  
LINK        ZN    ZN A1001                 OE1 GLU A 395     1555   1555  2.26  
LINK        ZN    ZN A1001                 NE2 HIS A 371     1555   1555  2.16  
LINK         O4  NAG A1617                 C1  NAG A1618     1555   1555  1.45  
LINK         O4  NAG A1618                 C1  BMA A1619     1555   1555  1.45  
LINK         O6  BMA A1619                 C1  MAN A1620     1555   1555  1.44  
LINK         O3  BMA A1619                 C1  MAN A1623     1555   1555  1.45  
LINK         O6  MAN A1623                 C1  BMA A1624     1555   1555  1.44  
CISPEP   1 ASP A  146    PRO A  147          0         5.86                     
SITE     1 AC1  4 HIS A 367  HIS A 371  GLU A 395  SLC A1626                    
SITE     1 AC2 11 GLN A 265  HIS A 337  ALA A 338  HIS A 367                    
SITE     2 AC2 11 GLU A 368  LYS A 495  HIS A 497  TYR A 504                    
SITE     3 AC2 11 TYR A 507   ZN A1001  HOH A2103                               
SITE     1 AC3 18 ASN A  53  THR A  55  GLU A  57  ASN A  58                    
SITE     2 AC3 18 ARG A 157  ASN A 196  ARG A 238  LYS A 241                    
SITE     3 AC3 18 HIS A 242  TYR A 243  PRO A 278  ASN A 311                    
SITE     4 AC3 18 ASP A 330  ARG A 332  ALA A 546  HOH A2091                    
SITE     5 AC3 18 HOH A2199  HOH A2200                                          
CRYST1  173.797  173.797  100.795  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      0.005754  0.003322  0.000000        0.00000                         
SCALE2      0.000000  0.006644  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009921        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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