spacer
spacer

PDBsum entry 1j37

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
1j37
Jmol
Contents
Protein chains
598 a.a. *
Ligands
X8Z ×2
Metals
_ZN ×2
* Residue conservation analysis
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   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   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
      
PROCHECK
Go to PROCHECK summary
 References