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Database: PDB
Entry: 1J37
LinkDB: 1J37
Original site: 1J37 
HEADER    HYDROLASE                               20-JAN-03   1J37              
TITLE     CRYSTAL STRUCTURE OF DROSOPHILA ANCE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN CONVERTING ENZYME;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ANCE;                                                       
COMPND   5 EC: 3.4.15.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    ANGIOTENSIN, HYDROLASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.M.KIM,D.R.SHIN,O.J.YOO,H.LEE,J.-O.LEE                               
REVDAT   4   08-MAY-13 1J37    1       HET    HETATM HETNAM VERSN               
REVDAT   3   24-FEB-09 1J37    1       VERSN                                    
REVDAT   2   01-FEB-05 1J37    1       JRNL                                     
REVDAT   1   20-JUL-03 1J37    0                                                
JRNL        AUTH   H.M.KIM,D.R.SHIN,O.J.YOO,H.LEE,J.-O.LEE                      
JRNL        TITL   CRYSTAL STRUCTURE OF DROSOPHILA ANGIOTENSIN I-CONVERTING     
JRNL        TITL 2 ENZYME BOUND TO CAPTOPRIL AND LISINOPRIL                     
JRNL        REF    FEBS LETT.                    V. 538    65 2003              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   12633854                                                     
JRNL        DOI    10.1016/S0014-5793(03)00128-5                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 82133                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4106                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9800                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1J37 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JAN-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB005573.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-DEC-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 123                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9280                             
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82133                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE 7.2M, PH 7.5, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       60.61150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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     VAL A    14                                                      
REMARK 465     THR A    15                                                      
REMARK 465     GLN A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     LYS A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     THR B    15                                                      
REMARK 465     GLN B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     VAL B    19                                                      
REMARK 465     LYS B    20                                                      
REMARK 465     GLU B    21                                                      
REMARK 465     GLU B    22                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     GLY A   233                                                      
REMARK 475     ALA A   435                                                      
REMARK 475     GLY A   579                                                      
REMARK 475     ALA A   581                                                      
REMARK 475     GLY B   233                                                      
REMARK 475     ALA B   435                                                      
REMARK 475     GLY B   579                                                      
REMARK 475     ALA B   581                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     TYR A  228   N    CA   C    O    CB                              
REMARK 480     GLN A  229   N    CA   C    O    CB                              
REMARK 480     GLN A  230   N    CA   C    O    CB                              
REMARK 480     ILE A  231   N    CA   C    O                                    
REMARK 480     HIS A  232   N    CA   C    O    CB                              
REMARK 480     TYR A  234   N    CA   C    O    CB                              
REMARK 480     VAL A  235   N    CA   C    O    CB                              
REMARK 480     ARG A  236   N    CA   C    O    CB                              
REMARK 480     PHE A  237   N    CA   C    O    CB                              
REMARK 480     ARG A  238   N    CA   C    O    CB                              
REMARK 480     ARG A  427   N    CA   C    O    CB                              
REMARK 480     ILE A  428   N    CA   C    O    CB                              
REMARK 480     ASN A  429   N    CA   C    O    CB                              
REMARK 480     GLN A  430   N    CA   C    O    CB                              
REMARK 480     LEU A  431   N    CA   C    O    CB                              
REMARK 480     PHE A  432   N    CA   C    O    CB                              
REMARK 480     LEU A  433   N    CA   C    O    CB                              
REMARK 480     THR A  434   N    CA   C    O    CB                              
REMARK 480     LEU A  436   N    CA   C    O    CB                              
REMARK 480     ASP A  437   N    CA   C    O    CB                              
REMARK 480     LYS A  580   N    CA   C    O    CB                              
REMARK 480     ILE A  582   N    CA   C    O    CB                              
REMARK 480     ALA A  583   N    CA   C    O                                    
REMARK 480     GLU A  584   N    CA   C    O    CB                              
REMARK 480     TYR A  585   N    CA   C    O    CB                              
REMARK 480     TRP A  592   N    CA   C    O                                    
REMARK 480     LEU A  593   N    CA   C    O                                    
REMARK 480     GLU A  594   N    CA   C    O    CB                              
REMARK 480     TYR B  228   N    CA   C    O    CB                              
REMARK 480     GLN B  229   N    CA   C    O    CB                              
REMARK 480     GLN B  230   N    CA   C    O    CB                              
REMARK 480     ILE B  231   N    CA   C    O                                    
REMARK 480     HIS B  232   N    CA   C    O    CB                              
REMARK 480     TYR B  234   N    CA   C    O    CB                              
REMARK 480     VAL B  235   N    CA   C    O    CB                              
REMARK 480     ARG B  236   N    CA   C    O    CB                              
REMARK 480     PHE B  237   N    CA   C    O    CB                              
REMARK 480     ARG B  238   N    CA   C    O    CB                              
REMARK 480     ARG B  427   N    CA   C    O    CB                              
REMARK 480     ILE B  428   N    CA   C    O    CB                              
REMARK 480     ASN B  429   N    CA   C    O    CB                              
REMARK 480     GLN B  430   N    CA   C    O    CB                              
REMARK 480     LEU B  431   N    CA   C    O    CB                              
REMARK 480     PHE B  432   N    CA   C    O    CB                              
REMARK 480     LEU B  433   N    CA   C    O    CB                              
REMARK 480     THR B  434   N    CA   C    O    CB                              
REMARK 480     LEU B  436   N    CA   C    O    CB                              
REMARK 480     ASP B  437   N    CA   C    O    CB                              
REMARK 480     LYS B  580   N    CA   C    O    CB                              
REMARK 480     ILE B  582   N    CA   C    O    CB                              
REMARK 480     ALA B  583   N    CA   C    O                                    
REMARK 480     GLU B  584   N    CA   C    O    CB                              
REMARK 480     TYR B  585   N    CA   C    O    CB                              
REMARK 480     TRP B  592   N    CA   C    O                                    
REMARK 480     LEU B  593   N    CA   C    O                                    
REMARK 480     GLU B  594   N    CA   C    O    CB                              
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   O    MET B   256     N    LEU B   258              2.08            
REMARK 500   O    MET A   256     N    LEU A   258              2.10            
REMARK 500   O    ASP B   541     N    TYR B   543              2.15            
REMARK 500   O    ASP A   541     N    TYR A   543              2.15            
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    ALA A  53       97.96   -164.28                                   
REMARK 500    TYR A  88      178.78    -50.90                                   
REMARK 500    GLN A  89      -75.89    -91.75                                   
REMARK 500    GLU A  91     -152.38    -71.12                                   
REMARK 500    ASP A  92      -63.78     66.15                                   
REMARK 500    ASP A 137       76.28   -166.41                                   
REMARK 500    SER A 138       -0.97    -54.06                                   
REMARK 500    LYS A 140      -73.91    -57.35                                   
REMARK 500    ASP A 146      -81.33    -49.58                                   
REMARK 500    PRO A 147      -93.21    -58.98                                   
REMARK 500    ALA A 176      -19.35    -45.35                                   
REMARK 500    SER A 199     -174.55   -171.55                                   
REMARK 500    GLU A 209       56.28     37.40                                   
REMARK 500    GLN A 229       57.72    -98.73                                   
REMARK 500    GLN A 230      -30.61   -157.04                                   
REMARK 500    THR A 251      -13.23     62.19                                   
REMARK 500    MET A 256     -143.74    -60.13                                   
REMARK 500    HIS A 257      -15.66     44.07                                   
REMARK 500    ALA A 338      141.37    -30.14                                   
REMARK 500    LEU A 345     -140.69   -139.77                                   
REMARK 500    CYS A 354       45.35    -88.96                                   
REMARK 500    PHE A 383      -54.51    -16.49                                   
REMARK 500    ASN A 390      124.68     65.23                                   
REMARK 500    VAL A 397      -70.69    -37.47                                   
REMARK 500    LYS A 418      -85.01    -58.21                                   
REMARK 500    ARG A 422       43.95    -76.00                                   
REMARK 500    ASP A 423      -79.53    -14.35                                   
REMARK 500    ASP A 424      -49.97    159.55                                   
REMARK 500    TYR A 496      -58.45    -29.59                                   
REMARK 500    ASP A 531      -84.95    -51.11                                   
REMARK 500    VAL A 533     -158.76    -92.35                                   
REMARK 500    GLU A 534       -1.89     68.82                                   
REMARK 500    ASN A 539       22.71   -142.46                                   
REMARK 500    ILE A 542       -0.55     38.39                                   
REMARK 500    ALA A 560       -6.07     58.95                                   
REMARK 500    ALA A 581      -50.01   -170.96                                   
REMARK 500    ASN A 601       62.34     60.55                                   
REMARK 500    THR A 608      155.05    -49.63                                   
REMARK 500    VAL A 613     -129.72   -143.38                                   
REMARK 500    SER A 615     -144.70     60.71                                   
REMARK 500    HIS A 616      104.72     87.26                                   
REMARK 500    ALA B  53       96.99   -165.02                                   
REMARK 500    TYR B  88      178.81    -49.41                                   
REMARK 500    GLN B  89      -76.40    -92.58                                   
REMARK 500    GLU B  91     -152.87    -69.83                                   
REMARK 500    ASP B  92      -65.08     66.19                                   
REMARK 500    ASP B 137       78.26   -164.39                                   
REMARK 500    SER B 138       -1.24    -56.31                                   
REMARK 500    LYS B 140      -74.12    -57.65                                   
REMARK 500    ASP B 146      -79.36    -51.20                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      84 RAMACHANDRAN OUTLIERS.                        
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 A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 371   NE2                                                    
REMARK 620 2 GLU A 395   OE1 107.6                                              
REMARK 620 3 HIS A 367   NE2 100.3  88.5                                        
REMARK 620 4 X8Z A 801   S    94.0 145.9 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 371   NE2                                                    
REMARK 620 2 GLU B 395   OE1 107.7                                              
REMARK 620 3 HIS B 367   NE2 100.5  86.1                                        
REMARK 620 4 X8Z B 802   S    94.5 146.5 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: L-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     X8Z A   801                                                      
REMARK 630     X8Z B   802                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    PRO CC8                                                  
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 A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X8Z A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X8Z B 802                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1J36   RELATED DB: PDB                                   
REMARK 900 DROSOPHILA ANCE WITH LISINOPRIL                                      
REMARK 900 RELATED ID: 1J38   RELATED DB: PDB                                   
REMARK 900 DROSOPHILA ANCE                                                      
DBREF  1J37 A   14   615  UNP    Q10714   ACE_DROME       14    615             
DBREF  1J37 B   14   615  UNP    Q10714   ACE_DROME       14    615             
SEQADV 1J37 ARG A   51  UNP  Q10714    GLY    51 CONFLICT                       
SEQADV 1J37 ALA A   53  UNP  Q10714    ASN    53 CONFLICT                       
SEQADV 1J37 ILE A  607  UNP  Q10714    THR   607 CONFLICT                       
SEQADV 1J37 HIS A  616  UNP  Q10714              EXPRESSION TAG                 
SEQADV 1J37 HIS A  617  UNP  Q10714              EXPRESSION TAG                 
SEQADV 1J37 HIS A  618  UNP  Q10714              EXPRESSION TAG                 
SEQADV 1J37 HIS A  619  UNP  Q10714              EXPRESSION TAG                 
SEQADV 1J37 HIS A  620  UNP  Q10714              EXPRESSION TAG                 
SEQADV 1J37 ARG B   51  UNP  Q10714    GLY    51 CONFLICT                       
SEQADV 1J37 ALA B   53  UNP  Q10714    ASN    53 CONFLICT                       
SEQADV 1J37 ILE B  607  UNP  Q10714    THR   607 CONFLICT                       
SEQADV 1J37 HIS B  616  UNP  Q10714              EXPRESSION TAG                 
SEQADV 1J37 HIS B  617  UNP  Q10714              EXPRESSION TAG                 
SEQADV 1J37 HIS B  618  UNP  Q10714              EXPRESSION TAG                 
SEQADV 1J37 HIS B  619  UNP  Q10714              EXPRESSION TAG                 
SEQADV 1J37 HIS B  620  UNP  Q10714              EXPRESSION TAG                 
SEQRES   1 A  607  VAL THR GLN ALA LEU VAL LYS GLU GLU ILE GLN ALA LYS          
SEQRES   2 A  607  GLU TYR LEU GLU ASN LEU ASN LYS GLU LEU ALA LYS ARG          
SEQRES   3 A  607  THR ASN VAL GLU THR GLU ALA ALA TRP ALA TYR ARG SER          
SEQRES   4 A  607  ALA ILE THR ASP GLU ASN GLU LYS LYS LYS ASN GLU ILE          
SEQRES   5 A  607  SER ALA GLU LEU ALA LYS PHE MET LYS GLU VAL ALA SER          
SEQRES   6 A  607  ASP THR THR LYS PHE GLN TRP ARG SER TYR GLN SER GLU          
SEQRES   7 A  607  ASP LEU LYS ARG GLN PHE LYS ALA LEU THR LYS LEU GLY          
SEQRES   8 A  607  TYR ALA ALA LEU PRO GLU ASP ASP TYR ALA GLU LEU LEU          
SEQRES   9 A  607  ASP THR LEU SER ALA MET GLU SER ASN PHE ALA LYS VAL          
SEQRES  10 A  607  LYS VAL CYS ASP TYR LYS ASP SER THR LYS CYS ASP LEU          
SEQRES  11 A  607  ALA LEU ASP PRO GLU ILE GLU GLU VAL ILE SER LYS SER          
SEQRES  12 A  607  ARG ASP HIS GLU GLU LEU ALA TYR TYR TRP ARG GLU PHE          
SEQRES  13 A  607  TYR ASP LYS ALA GLY THR ALA VAL ARG SER GLN PHE GLU          
SEQRES  14 A  607  ARG TYR VAL GLU LEU ASN THR LYS ALA ALA LYS LEU ASN          
SEQRES  15 A  607  ASN PHE THR SER GLY ALA GLU ALA TRP LEU ASP GLU TYR          
SEQRES  16 A  607  GLU ASP ASP THR PHE GLU GLN GLN LEU GLU ASP ILE PHE          
SEQRES  17 A  607  ALA ASP ILE ARG PRO LEU TYR GLN GLN ILE HIS GLY TYR          
SEQRES  18 A  607  VAL ARG PHE ARG LEU ARG LYS HIS TYR GLY ASP ALA VAL          
SEQRES  19 A  607  VAL SER GLU THR GLY PRO ILE PRO MET HIS LEU LEU GLY          
SEQRES  20 A  607  ASN MET TRP ALA GLN GLN TRP SER GLU ILE ALA ASP ILE          
SEQRES  21 A  607  VAL SER PRO PHE PRO GLU LYS PRO LEU VAL ASP VAL SER          
SEQRES  22 A  607  ALA GLU MET GLU LYS GLN ALA TYR THR PRO LEU LYS MET          
SEQRES  23 A  607  PHE GLN MET GLY ASP ASP PHE PHE THR SER MET ASN LEU          
SEQRES  24 A  607  THR LYS LEU PRO GLN ASP PHE TRP ASP LYS SER ILE ILE          
SEQRES  25 A  607  GLU LYS PRO THR ASP GLY ARG ASP LEU VAL CYS HIS ALA          
SEQRES  26 A  607  SER ALA TRP ASP PHE TYR LEU ILE ASP ASP VAL ARG ILE          
SEQRES  27 A  607  LYS GLN CYS THR ARG VAL THR GLN ASP GLN LEU PHE THR          
SEQRES  28 A  607  VAL HIS HIS GLU LEU GLY HIS ILE GLN TYR PHE LEU GLN          
SEQRES  29 A  607  TYR GLN HIS GLN PRO PHE VAL TYR ARG THR GLY ALA ASN          
SEQRES  30 A  607  PRO GLY PHE HIS GLU ALA VAL GLY ASP VAL LEU SER LEU          
SEQRES  31 A  607  SER VAL SER THR PRO LYS HIS LEU GLU LYS ILE GLY LEU          
SEQRES  32 A  607  LEU LYS ASP TYR VAL ARG ASP ASP GLU ALA ARG ILE ASN          
SEQRES  33 A  607  GLN LEU PHE LEU THR ALA LEU ASP LYS ILE VAL PHE LEU          
SEQRES  34 A  607  PRO PHE ALA PHE THR MET ASP LYS TYR ARG TRP SER LEU          
SEQRES  35 A  607  PHE ARG GLY GLU VAL ASP LYS ALA ASN TRP ASN CYS ALA          
SEQRES  36 A  607  PHE TRP LYS LEU ARG ASP GLU TYR SER GLY ILE GLU PRO          
SEQRES  37 A  607  PRO VAL VAL ARG SER GLU LYS ASP PHE ASP ALA PRO ALA          
SEQRES  38 A  607  LYS TYR HIS ILE SER ALA ASP VAL GLU TYR LEU ARG TYR          
SEQRES  39 A  607  LEU VAL SER PHE ILE ILE GLN PHE GLN PHE TYR LYS SER          
SEQRES  40 A  607  ALA CYS ILE LYS ALA GLY GLN TYR ASP PRO ASP ASN VAL          
SEQRES  41 A  607  GLU LEU PRO LEU ASP ASN CYS ASP ILE TYR GLY SER ALA          
SEQRES  42 A  607  ARG ALA GLY ALA ALA PHE HIS ASN MET LEU SER MET GLY          
SEQRES  43 A  607  ALA SER LYS PRO TRP PRO ASP ALA LEU GLU ALA PHE ASN          
SEQRES  44 A  607  GLY GLU ARG ILE MET SER GLY LYS ALA ILE ALA GLU TYR          
SEQRES  45 A  607  PHE GLU PRO LEU ARG VAL TRP LEU GLU ALA GLU ASN ILE          
SEQRES  46 A  607  LYS ASN ASN VAL HIS ILE GLY TRP ILE THR SER ASN LYS          
SEQRES  47 A  607  CYS VAL SER SER HIS HIS HIS HIS HIS                          
SEQRES   1 B  607  VAL THR GLN ALA LEU VAL LYS GLU GLU ILE GLN ALA LYS          
SEQRES   2 B  607  GLU TYR LEU GLU ASN LEU ASN LYS GLU LEU ALA LYS ARG          
SEQRES   3 B  607  THR ASN VAL GLU THR GLU ALA ALA TRP ALA TYR ARG SER          
SEQRES   4 B  607  ALA ILE THR ASP GLU ASN GLU LYS LYS LYS ASN GLU ILE          
SEQRES   5 B  607  SER ALA GLU LEU ALA LYS PHE MET LYS GLU VAL ALA SER          
SEQRES   6 B  607  ASP THR THR LYS PHE GLN TRP ARG SER TYR GLN SER GLU          
SEQRES   7 B  607  ASP LEU LYS ARG GLN PHE LYS ALA LEU THR LYS LEU GLY          
SEQRES   8 B  607  TYR ALA ALA LEU PRO GLU ASP ASP TYR ALA GLU LEU LEU          
SEQRES   9 B  607  ASP THR LEU SER ALA MET GLU SER ASN PHE ALA LYS VAL          
SEQRES  10 B  607  LYS VAL CYS ASP TYR LYS ASP SER THR LYS CYS ASP LEU          
SEQRES  11 B  607  ALA LEU ASP PRO GLU ILE GLU GLU VAL ILE SER LYS SER          
SEQRES  12 B  607  ARG ASP HIS GLU GLU LEU ALA TYR TYR TRP ARG GLU PHE          
SEQRES  13 B  607  TYR ASP LYS ALA GLY THR ALA VAL ARG SER GLN PHE GLU          
SEQRES  14 B  607  ARG TYR VAL GLU LEU ASN THR LYS ALA ALA LYS LEU ASN          
SEQRES  15 B  607  ASN PHE THR SER GLY ALA GLU ALA TRP LEU ASP GLU TYR          
SEQRES  16 B  607  GLU ASP ASP THR PHE GLU GLN GLN LEU GLU ASP ILE PHE          
SEQRES  17 B  607  ALA ASP ILE ARG PRO LEU TYR GLN GLN ILE HIS GLY TYR          
SEQRES  18 B  607  VAL ARG PHE ARG LEU ARG LYS HIS TYR GLY ASP ALA VAL          
SEQRES  19 B  607  VAL SER GLU THR GLY PRO ILE PRO MET HIS LEU LEU GLY          
SEQRES  20 B  607  ASN MET TRP ALA GLN GLN TRP SER GLU ILE ALA ASP ILE          
SEQRES  21 B  607  VAL SER PRO PHE PRO GLU LYS PRO LEU VAL ASP VAL SER          
SEQRES  22 B  607  ALA GLU MET GLU LYS GLN ALA TYR THR PRO LEU LYS MET          
SEQRES  23 B  607  PHE GLN MET GLY ASP ASP PHE PHE THR SER MET ASN LEU          
SEQRES  24 B  607  THR LYS LEU PRO GLN ASP PHE TRP ASP LYS SER ILE ILE          
SEQRES  25 B  607  GLU LYS PRO THR ASP GLY ARG ASP LEU VAL CYS HIS ALA          
SEQRES  26 B  607  SER ALA TRP ASP PHE TYR LEU ILE ASP ASP VAL ARG ILE          
SEQRES  27 B  607  LYS GLN CYS THR ARG VAL THR GLN ASP GLN LEU PHE THR          
SEQRES  28 B  607  VAL HIS HIS GLU LEU GLY HIS ILE GLN TYR PHE LEU GLN          
SEQRES  29 B  607  TYR GLN HIS GLN PRO PHE VAL TYR ARG THR GLY ALA ASN          
SEQRES  30 B  607  PRO GLY PHE HIS GLU ALA VAL GLY ASP VAL LEU SER LEU          
SEQRES  31 B  607  SER VAL SER THR PRO LYS HIS LEU GLU LYS ILE GLY LEU          
SEQRES  32 B  607  LEU LYS ASP TYR VAL ARG ASP ASP GLU ALA ARG ILE ASN          
SEQRES  33 B  607  GLN LEU PHE LEU THR ALA LEU ASP LYS ILE VAL PHE LEU          
SEQRES  34 B  607  PRO PHE ALA PHE THR MET ASP LYS TYR ARG TRP SER LEU          
SEQRES  35 B  607  PHE ARG GLY GLU VAL ASP LYS ALA ASN TRP ASN CYS ALA          
SEQRES  36 B  607  PHE TRP LYS LEU ARG ASP GLU TYR SER GLY ILE GLU PRO          
SEQRES  37 B  607  PRO VAL VAL ARG SER GLU LYS ASP PHE ASP ALA PRO ALA          
SEQRES  38 B  607  LYS TYR HIS ILE SER ALA ASP VAL GLU TYR LEU ARG TYR          
SEQRES  39 B  607  LEU VAL SER PHE ILE ILE GLN PHE GLN PHE TYR LYS SER          
SEQRES  40 B  607  ALA CYS ILE LYS ALA GLY GLN TYR ASP PRO ASP ASN VAL          
SEQRES  41 B  607  GLU LEU PRO LEU ASP ASN CYS ASP ILE TYR GLY SER ALA          
SEQRES  42 B  607  ARG ALA GLY ALA ALA PHE HIS ASN MET LEU SER MET GLY          
SEQRES  43 B  607  ALA SER LYS PRO TRP PRO ASP ALA LEU GLU ALA PHE ASN          
SEQRES  44 B  607  GLY GLU ARG ILE MET SER GLY LYS ALA ILE ALA GLU TYR          
SEQRES  45 B  607  PHE GLU PRO LEU ARG VAL TRP LEU GLU ALA GLU ASN ILE          
SEQRES  46 B  607  LYS ASN ASN VAL HIS ILE GLY TRP ILE THR SER ASN LYS          
SEQRES  47 B  607  CYS VAL SER SER HIS HIS HIS HIS HIS                          
HET     ZN  A 701       1                                                       
HET     ZN  B 702       1                                                       
HET    X8Z  A 801      14                                                       
HET    X8Z  B 802      14                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     X8Z L-CAPTOPRIL                                                      
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5  X8Z    2(C9 H15 N O3 S)                                             
HELIX    1   1 ALA A   25  ARG A   51  1                                  27    
HELIX    2   2 THR A   55  THR A   80  1                                  26    
HELIX    3   3 GLN A   84  TYR A   88  5                                   5    
HELIX    4   4 ASP A   92  THR A  101  1                                  10    
HELIX    5   5 GLY A  104  LEU A  108  5                                   5    
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  LEU A  194  1                                  18    
HELIX   10  10 SER A  199  ASP A  206  1                                   8    
HELIX   11  11 GLU A  207  GLU A  209  5                                   3    
HELIX   12  12 THR A  212  GLY A  244  1                                  33    
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  TYR A  378  1                                  21    
HELIX   19  19 PRO A  382  ARG A  386  5                                   5    
HELIX   20  20 ALA A  389  THR A  407  1                                  19    
HELIX   21  21 THR A  407  ILE A  414  1                                   8    
HELIX   22  22 ASP A  424  ILE A  439  1                                  16    
HELIX   23  23 VAL A  440  ARG A  457  1                                  18    
HELIX   24  24 ASP A  461  ALA A  463  5                                   3    
HELIX   25  25 ASN A  464  GLY A  478  1                                  15    
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 ALA A  581  PHE A  586  1                                   6    
HELIX   33  33 PHE A  586  ASN A  600  1                                  15    
HELIX   34  34 ALA B   25  ARG B   51  1                                  27    
HELIX   35  35 THR B   55  THR B   80  1                                  26    
HELIX   36  36 GLN B   84  TYR B   88  5                                   5    
HELIX   37  37 ASP B   92  THR B  101  1                                  10    
HELIX   38  38 GLY B  104  LEU B  108  5                                   5    
HELIX   39  39 PRO B  109  LYS B  129  1                                  21    
HELIX   40  40 PRO B  147  SER B  156  1                                  10    
HELIX   41  41 ASP B  158  GLY B  174  1                                  17    
HELIX   42  42 VAL B  177  LEU B  194  1                                  18    
HELIX   43  43 SER B  199  ASP B  206  1                                   8    
HELIX   44  44 GLU B  207  GLU B  209  5                                   3    
HELIX   45  45 THR B  212  GLY B  244  1                                  33    
HELIX   46  46 TRP B  267  GLU B  269  5                                   3    
HELIX   47  47 ILE B  270  SER B  275  1                                   6    
HELIX   48  48 VAL B  285  GLN B  292  1                                   8    
HELIX   49  49 THR B  295  MET B  310  1                                  16    
HELIX   50  50 PRO B  316  SER B  323  1                                   8    
HELIX   51  51 THR B  358  TYR B  378  1                                  21    
HELIX   52  52 PRO B  382  ARG B  386  5                                   5    
HELIX   53  53 ALA B  389  SER B  406  1                                  18    
HELIX   54  54 THR B  407  ILE B  414  1                                   8    
HELIX   55  55 ASP B  424  ILE B  439  1                                  16    
HELIX   56  56 VAL B  440  ARG B  457  1                                  18    
HELIX   57  57 ASP B  461  ALA B  463  5                                   3    
HELIX   58  58 ASN B  464  GLY B  478  1                                  15    
HELIX   59  59 ASP B  491  ALA B  494  5                                   4    
HELIX   60  60 LYS B  495  ALA B  500  1                                   6    
HELIX   61  61 TYR B  504  ALA B  525  1                                  22    
HELIX   62  62 PRO B  536  CYS B  540  5                                   5    
HELIX   63  63 SER B  545  SER B  557  1                                  13    
HELIX   64  64 PRO B  563  GLY B  573  1                                  11    
HELIX   65  65 ALA B  581  PHE B  586  1                                   6    
HELIX   66  66 PHE B  586  ASN B  600  1                                  15    
SHEET    1   A 2 ILE A 254  PRO A 255  0                                        
SHEET    2   A 2 ILE A 479  GLU A 480  1  O  GLU A 480   N  ILE A 254           
SHEET    1   B 2 SER A 339  ASP A 342  0                                        
SHEET    2   B 2 VAL A 349  LYS A 352 -1  O  ARG A 350   N  TRP A 341           
SHEET    1   C 2 ARG A 485  SER A 486  0                                        
SHEET    2   C 2 CYS A 612  VAL A 613  1  O  VAL A 613   N  ARG A 485           
SHEET    1   D 2 ILE B 254  PRO B 255  0                                        
SHEET    2   D 2 ILE B 479  GLU B 480  1  O  GLU B 480   N  ILE B 254           
SHEET    1   E 2 SER B 339  ASP B 342  0                                        
SHEET    2   E 2 VAL B 349  LYS B 352 -1  O  ARG B 350   N  TRP B 341           
SHEET    1   F 2 ARG B 485  SER B 486  0                                        
SHEET    2   F 2 CYS B 612  VAL B 613  1  O  VAL B 613   N  ARG B 485           
SSBOND   1 CYS A  133    CYS A  141                          1555   1555  2.04  
SSBOND   2 CYS A  336    CYS A  354                          1555   1555  2.01  
SSBOND   3 CYS A  467    CYS A  612                          1555   1555  2.04  
SSBOND   4 CYS A  522    CYS A  540                          1555   1555  2.03  
SSBOND   5 CYS B  133    CYS B  141                          1555   1555  2.04  
SSBOND   6 CYS B  336    CYS B  354                          1555   1555  2.01  
SSBOND   7 CYS B  467    CYS B  612                          1555   1555  2.04  
SSBOND   8 CYS B  522    CYS B  540                          1555   1555  2.04  
LINK        ZN    ZN A 701                 NE2 HIS A 371     1555   1555  2.17  
LINK        ZN    ZN A 701                 OE1 GLU A 395     1555   1555  1.84  
LINK        ZN    ZN B 702                 NE2 HIS B 371     1555   1555  2.13  
LINK        ZN    ZN B 702                 OE1 GLU B 395     1555   1555  1.84  
LINK        ZN    ZN A 701                 NE2 HIS A 367     1555   1555  2.29  
LINK        ZN    ZN B 702                 NE2 HIS B 367     1555   1555  2.30  
LINK        ZN    ZN A 701                 S   X8Z A 801     1555   1555  1.99  
LINK        ZN    ZN B 702                 S   X8Z B 802     1555   1555  2.05  
SITE     1 AC1  4 HIS A 367  HIS A 371  GLU A 395  X8Z A 801                    
SITE     1 AC2  4 HIS B 367  HIS B 371  GLU B 395  X8Z B 802                    
SITE     1 AC3 12 GLN A 265  HIS A 337  ALA A 338  HIS A 367                    
SITE     2 AC3 12 GLU A 368  HIS A 371  GLU A 395  LYS A 495                    
SITE     3 AC3 12 HIS A 497  TYR A 504  TYR A 507   ZN A 701                    
SITE     1 AC4 12 GLN B 265  HIS B 337  ALA B 338  HIS B 367                    
SITE     2 AC4 12 GLU B 368  HIS B 371  GLU B 395  LYS B 495                    
SITE     3 AC4 12 HIS B 497  TYR B 504  TYR B 507   ZN B 702                    
CRYST1   94.912  121.223   94.740  90.00  99.39  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010536  0.000000  0.001742        0.00000                         
SCALE2      0.000000  0.008249  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010698        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system