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PDBsum entry 2x8y

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Hydrolase PDB id
2x8y
Jmol
Contents
Protein chain
595 a.a.
Ligands
FLC
NAG-NAG-BMA-MAN
NAG ×2
MAN-BMA
Metals
_ZN
Waters ×626
HEADER    HYDROLASE                               14-MAR-10   2X8Y
TITLE     CRYSTAL STRUCTURE OF ANCE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANGIOTENSIN CONVERTING ENZYME;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 17-614;
COMPND   5 SYNONYM: DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II;
COMPND   6 EC: 3.4.15.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE   3 ORGANISM_TAXID: 7227;
SOURCE   4 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 644223;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PPIC9
KEYWDS    HYDROLASE, ACE INHIBITOR, ZINC METALLOPEPTIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.AKIF,D.GEORGIADIS,A.MAHAJAN,V.DIVE,E.D.STURROCK,R.E.ISAAC,
AUTHOR   2 K.R.ACHARYA
REVDAT   2   21-JUL-10 2X8Y    1       JRNL   ATOM
REVDAT   1   02-JUN-10 2X8Y    0
JRNL        AUTH   M.AKIF,D.GEORGIADIS,A.MAHAJAN,V.DIVE,E.D.STURROCK,
JRNL        AUTH 2 R.E.ISAAC,K.R.ACHARYA
JRNL        TITL   HIGH RESOLUTION CRYSTAL STRUCTURES OF DROSOPHILA
JRNL        TITL 2 MELANOGASTER ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH
JRNL        TITL 3 NOVEL INHIBITORS AND ANTI- HYPERTENSIVE DRUGS.
JRNL        REF    J.MOL.BIOL.                   V. 400   502 2010
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   20488190
JRNL        DOI    10.1016/J.JMB.2010.05.024
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0072
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.27
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.13
REMARK   3   NUMBER OF REFLECTIONS             : 83371
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.19535
REMARK   3   R VALUE            (WORKING SET) : 0.19405
REMARK   3   FREE R VALUE                     : 0.22045
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 4406
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.900
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.949
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5630
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.89
REMARK   3   BIN R VALUE           (WORKING SET) : 0.301
REMARK   3   BIN FREE R VALUE SET COUNT          : 314
REMARK   3   BIN FREE R VALUE                    : 0.328
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4877
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 114
REMARK   3   SOLVENT ATOMS            : 626
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 29.5
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.914
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00
REMARK   3    B22 (A**2) : 0.00
REMARK   3    B33 (A**2) : 0.00
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.115
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.083
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.876
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5126 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6963 ; 0.982 ; 1.967
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   600 ; 4.812 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   263 ;34.176 ;24.677
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   856 ;12.304 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;15.098 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   748 ; 0.076 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3931 ; 0.004 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2983 ; 0.329 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4808 ; 0.650 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2143 ; 1.029 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2152 ; 1.756 ; 4.500
REMARK   3
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3   RIDING POSITIONS. THREE RESIDUES AT N-TERMINAL WERE EXCLUDED
REMARK   3   DUE TO INSUFFICIENT DENSITY.
REMARK   4
REMARK   4 2X8Y COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-10.
REMARK 100 THE PDBE ID CODE IS EBI-43247.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-JULY-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : DIAMOND
REMARK 200  BEAMLINE                       : I03
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 89453
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.90
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0
REMARK 200  DATA REDUNDANCY                : 4.3
REMARK 200  R MERGE                    (I) : 0.07
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.3
REMARK 200  R MERGE FOR SHELL          (I) : 0.21
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 6.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1J38
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 71.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       86.54800
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.96851
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       33.85533
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       86.54800
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       49.96851
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       33.85533
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       86.54800
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       49.96851
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       33.85533
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       99.93702
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       67.71067
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       99.93702
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       67.71067
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       99.93702
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       67.71067
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ALA A    17
REMARK 465     LEU A    18
REMARK 465     VAL A    19
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LYS A  20    CG   CD   CE   NZ
REMARK 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 CSSEQI  ATOMS
REMARK 480     GLN A  24    CG   CD  OE1  NE2
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   O4   NAG A  1622     O    HOH A  2625              2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A  53       85.14   -161.41
REMARK 500    SER A 138        0.29    -68.38
REMARK 500    LEU A 345     -132.19   -109.72
REMARK 500    ASN A 572       10.45   -141.06
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 A1616  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2615   O
REMARK 620 2 HIS A 371   NE2 132.4
REMARK 620 3 GLU A 395   OE1 104.6 100.3
REMARK 620 4 HIS A 367   NE2 111.5 104.6  97.2
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A1615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800     SUGAR BOUND TO ASN A 196 RESIDUES 1617 TO 1624
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J38   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF DROSOPHILA ANCE
REMARK 900 RELATED ID: 1J36   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF DROSOPHILA ANCE
REMARK 900 RELATED ID: 1J37   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF DROSOPHILA ANCE
REMARK 900 RELATED ID: 2X94   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ANCE-PERINDOPRILAT COMPLEX
REMARK 900 RELATED ID: 2X8Z   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ANCE-CAPTOPRIL COMPLEX
REMARK 900 RELATED ID: 2X91   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ANCE-LISINOPRIL COMPLEX
REMARK 900 RELATED ID: 2X95   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ANCE-LISINOPRIL-
REMARK 900  TRYPTOPHAN ANALOGUE, LISW-S COMPLEX
REMARK 900 RELATED ID: 2X92   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ANCE-RAMIPRILAT COMPLEX
REMARK 900 RELATED ID: 2X96   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ANCE-RXPA380 COMPLEX
REMARK 900 RELATED ID: 2X97   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ANCE-RXP407 COMPLEX
REMARK 900 RELATED ID: 2X93   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ANCE-TRANDOLAPRILAT COMPLEX
REMARK 900 RELATED ID: 2X90   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF ANCE-ENALAPRILAT COMPLEX
DBREF  2X8Y A   17   614  UNP    Q10714   ACE_DROME       17    614
SEQRES   1 A  598  ALA LEU VAL LYS GLU GLU ILE GLN ALA LYS GLU TYR LEU
SEQRES   2 A  598  GLU ASN LEU ASN LYS GLU LEU ALA LYS ARG THR ASN VAL
SEQRES   3 A  598  GLU THR GLU ALA ALA TRP ALA TYR GLY SER ASN ILE THR
SEQRES   4 A  598  ASP GLU ASN GLU LYS LYS LYS ASN GLU ILE SER ALA GLU
SEQRES   5 A  598  LEU ALA LYS PHE MET LYS GLU VAL ALA SER ASP THR THR
SEQRES   6 A  598  LYS PHE GLN TRP ARG SER TYR GLN SER GLU ASP LEU LYS
SEQRES   7 A  598  ARG GLN PHE LYS ALA LEU THR LYS LEU GLY TYR ALA ALA
SEQRES   8 A  598  LEU PRO GLU ASP ASP TYR ALA GLU LEU LEU ASP THR LEU
SEQRES   9 A  598  SER ALA MET GLU SER ASN PHE ALA LYS VAL LYS VAL CYS
SEQRES  10 A  598  ASP TYR LYS ASP SER THR LYS CYS ASP LEU ALA LEU ASP
SEQRES  11 A  598  PRO GLU ILE GLU GLU VAL ILE SER LYS SER ARG ASP HIS
SEQRES  12 A  598  GLU GLU LEU ALA TYR TYR TRP ARG GLU PHE TYR ASP LYS
SEQRES  13 A  598  ALA GLY THR ALA VAL ARG SER GLN PHE GLU ARG TYR VAL
SEQRES  14 A  598  GLU LEU ASN THR LYS ALA ALA LYS LEU ASN ASN PHE THR
SEQRES  15 A  598  SER GLY ALA GLU ALA TRP LEU ASP GLU TYR GLU ASP ASP
SEQRES  16 A  598  THR PHE GLU GLN GLN LEU GLU ASP ILE PHE ALA ASP ILE
SEQRES  17 A  598  ARG PRO LEU TYR GLN GLN ILE HIS GLY TYR VAL ARG PHE
SEQRES  18 A  598  ARG LEU ARG LYS HIS TYR GLY ASP ALA VAL VAL SER GLU
SEQRES  19 A  598  THR GLY PRO ILE PRO MET HIS LEU LEU GLY ASN MET TRP
SEQRES  20 A  598  ALA GLN GLN TRP SER GLU ILE ALA ASP ILE VAL SER PRO
SEQRES  21 A  598  PHE PRO GLU LYS PRO LEU VAL ASP VAL SER ALA GLU MET
SEQRES  22 A  598  GLU LYS GLN GLY TYR THR PRO LEU LYS MET PHE GLN MET
SEQRES  23 A  598  GLY ASP ASP PHE PHE THR SER MET ASN LEU THR LYS LEU
SEQRES  24 A  598  PRO GLN ASP PHE TRP ASP LYS SER ILE ILE GLU LYS PRO
SEQRES  25 A  598  THR ASP GLY ARG ASP LEU VAL CYS HIS ALA SER ALA TRP
SEQRES  26 A  598  ASP PHE TYR LEU THR ASP ASP VAL ARG ILE LYS GLN CYS
SEQRES  27 A  598  THR ARG VAL THR GLN ASP GLN LEU PHE THR VAL HIS HIS
SEQRES  28 A  598  GLU LEU GLY HIS ILE GLN TYR PHE LEU GLN TYR GLN HIS
SEQRES  29 A  598  GLN PRO PHE VAL TYR ARG THR GLY ALA ASN PRO GLY PHE
SEQRES  30 A  598  HIS GLU ALA VAL GLY ASP VAL LEU SER LEU SER VAL SER
SEQRES  31 A  598  THR PRO LYS HIS LEU GLU LYS ILE GLY LEU LEU LYS ASP
SEQRES  32 A  598  TYR VAL ARG ASP ASP GLU ALA ARG ILE ASN GLN LEU PHE
SEQRES  33 A  598  LEU THR ALA LEU ASP LYS ILE VAL PHE LEU PRO PHE ALA
SEQRES  34 A  598  PHE THR MET ASP LYS TYR ARG TRP SER LEU PHE ARG GLY
SEQRES  35 A  598  GLU VAL ASP LYS ALA ASN TRP ASN CYS ALA PHE TRP LYS
SEQRES  36 A  598  LEU ARG ASP GLU TYR SER GLY ILE GLU PRO PRO VAL VAL
SEQRES  37 A  598  ARG SER GLU LYS ASP PHE ASP ALA PRO ALA LYS TYR HIS
SEQRES  38 A  598  ILE SER ALA ASP VAL GLU TYR LEU ARG TYR LEU VAL SER
SEQRES  39 A  598  PHE ILE ILE GLN PHE GLN PHE TYR LYS SER ALA CYS ILE
SEQRES  40 A  598  LYS ALA GLY GLN TYR ASP PRO ASP ASN VAL GLU LEU PRO
SEQRES  41 A  598  LEU ASP ASN CYS ASP ILE TYR GLY SER ALA ALA ALA GLY
SEQRES  42 A  598  ALA ALA PHE HIS ASN MET LEU SER MET GLY ALA SER LYS
SEQRES  43 A  598  PRO TRP PRO ASP ALA LEU GLU ALA PHE ASN GLY GLU ARG
SEQRES  44 A  598  ILE MET SER GLY LYS ALA ILE ALA GLU TYR PHE GLU PRO
SEQRES  45 A  598  LEU ARG VAL TRP LEU GLU ALA GLU ASN ILE LYS ASN ASN
SEQRES  46 A  598  VAL HIS ILE GLY TRP THR THR SER ASN LYS CYS VAL SER
MODRES 2X8Y ASN A   53  ASN  GLYCOSYLATION SITE
MODRES 2X8Y ASN A  196  ASN  GLYCOSYLATION SITE
MODRES 2X8Y ASN A  311  ASN  GLYCOSYLATION SITE
HET    FLC  A1615      13
HET     ZN  A1616       1
HET    NAG  A1617      14
HET    NAG  A1618      14
HET    MAN  A1623      11
HET    BMA  A1619      11
HET    BMA  A1624      11
HET    MAN  A1620      11
HET    NAG  A1621      14
HET    NAG  A1622      14
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     FLC CITRATE ANION
HETNAM      ZN ZINC ION
HETNAM     BMA BETA-D-MANNOSE
FORMUL   2  FLC    C6 H5 O7 3-
FORMUL   3   ZN    ZN 2+
FORMUL   4  BMA    2(C6 H12 O6)
FORMUL   6  NAG    4(C8 H15 N O6)
FORMUL   7  MAN    2(C6 H12 O6)
FORMUL   8  HOH   *626(H2 O)
HELIX    1   1 GLU A   21  ASN A   53  1                                  33
HELIX    2   2 THR A   55  THR A   81  1                                  27
HELIX    3   3 GLN A   84  TYR A   88  5                                   5
HELIX    4   4 SER A   90  LYS A  102  1                                  13
HELIX    5   5 LEU A  103  LEU A  108  5                                   6
HELIX    6   6 PRO A  109  VAL A  130  1                                  22
HELIX    7   7 PRO A  147  SER A  156  1                                  10
HELIX    8   8 ASP A  158  GLY A  174  1                                  17
HELIX    9   9 VAL A  177  ASN A  195  1                                  19
HELIX   10  10 SER A  199  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 HIS A  257  LEU A  259  5                                   3
HELIX   14  14 TRP A  267  GLU A  269  5                                   3
HELIX   15  15 ILE A  270  SER A  275  1                                   6
HELIX   16  16 VAL A  285  GLN A  292  1                                   8
HELIX   17  17 THR A  295  MET A  310  1                                  16
HELIX   18  18 PRO A  316  SER A  323  1                                   8
HELIX   19  19 THR A  358  GLN A  379  1                                  22
HELIX   20  20 PRO A  382  ARG A  386  5                                   5
HELIX   21  21 ASN A  390  SER A  406  1                                  17
HELIX   22  22 THR A  407  ILE A  414  1                                   8
HELIX   23  23 ASP A  423  ILE A  439  1                                  17
HELIX   24  24 VAL A  440  ARG A  457  1                                  18
HELIX   25  25 ASP A  461  ALA A  463  5                                   3
HELIX   26  26 ASN A  464  GLY A  478  1                                  15
HELIX   27  27 ASP A  491  ALA A  494  5                                   4
HELIX   28  28 LYS A  495  ALA A  500  1                                   6
HELIX   29  29 TYR A  504  ALA A  525  1                                  22
HELIX   30  30 PRO A  536  CYS A  540  5                                   5
HELIX   31  31 SER A  545  SER A  557  1                                  13
HELIX   32  32 PRO A  563  GLY A  573  1                                  11
HELIX   33  33 GLY A  579  ASN A  600  1                                  22
SHEET    1  AA 2 LYS A 131  VAL A 132  0
SHEET    2  AA 2 LEU A 143  ALA A 144 -1  O  LEU A 143   N  VAL A 132
SHEET    1  AB 2 ILE A 254  PRO A 255  0
SHEET    2  AB 2 ILE A 479  GLU A 480  1  N  GLU A 480   O  ILE A 254
SHEET    1  AC 2 SER A 339  ASP A 342  0
SHEET    2  AC 2 VAL A 349  LYS A 352 -1  O  ARG A 350   N  TRP A 341
SHEET    1  AD 2 ARG A 485  SER A 486  0
SHEET    2  AD 2 CYS A 612  VAL A 613  1  N  VAL A 613   O  ARG A 485
SSBOND   1 CYS A  133    CYS A  141                          1555   1555  2.04
SSBOND   2 CYS A  336    CYS A  354                          1555   1555  2.03
SSBOND   3 CYS A  467    CYS A  612                          1555   1555  2.05
SSBOND   4 CYS A  522    CYS A  540                          1555   1555  2.03
LINK         ND2 ASN A  53                 C1  NAG A1622     1555   1555  1.48
LINK         ND2 ASN A 196                 C1  NAG A1617     1555   1555  1.44
LINK         ND2 ASN A 311                 C1  NAG A1621     1555   1555  1.44
LINK        ZN    ZN A1616                 OE1 GLU A 395     1555   1555  2.00
LINK        ZN    ZN A1616                 O   HOH A2615     1555   1555  2.02
LINK        ZN    ZN A1616                 NE2 HIS A 371     1555   1555  2.05
LINK        ZN    ZN A1616                 NE2 HIS A 367     1555   1555  2.11
LINK         O4  NAG A1617                 C1  NAG A1618     1555   1555  1.45
LINK         O4  NAG A1618                 C1  BMA A1619     1555   1555  1.45
LINK         O6  BMA A1619                 C1  MAN A1620     1555   1555  1.44
LINK         O3  BMA A1619                 C1  MAN A1623     1555   1555  1.44
LINK         O6  MAN A1623                 C1  BMA A1624     1555   1555  1.45
CISPEP   1 ASP A  146    PRO A  147          0         5.67
SITE     1 AC1 12 GLN A 265  HIS A 337  ALA A 338  HIS A 367
SITE     2 AC1 12 GLU A 368  LYS A 495  HIS A 497  TYR A 504
SITE     3 AC1 12 TYR A 507   ZN A1616  HOH A2613  HOH A2615
SITE     1 AC2  5 HIS A 367  HIS A 371  GLU A 395  FLC A1615
SITE     2 AC2  5 HOH A2615
SITE     1 AC3 28 ASN A  53  THR A  55  GLU A  57  ASN A  58
SITE     2 AC3 28 GLN A  84  ARG A 157  HIS A 159  ASN A 196
SITE     3 AC3 28 ARG A 238  LYS A 241  HIS A 242  TYR A 243
SITE     4 AC3 28 GLY A 244  PRO A 278  ASN A 311  ASP A 330
SITE     5 AC3 28 ARG A 332  HOH A2083  HOH A2319  HOH A2616
SITE     6 AC3 28 HOH A2617  HOH A2619  HOH A2620  HOH A2621
SITE     7 AC3 28 HOH A2622  HOH A2623  HOH A2625  HOH H2001
CRYST1  173.096  173.096  101.566  90.00  90.00 120.00 H 3           9
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.005777  0.003335  0.000000        0.00000
SCALE2      0.000000  0.006671  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009846        0.00000
      
PROCHECK
Go to PROCHECK summary
 References