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PDBsum entry 4apj

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase/hormone PDB id
4apj
Jmol
Contents
Protein chains
581 a.a.
11 a.a.
Ligands
SO4
PE4 ×3
NAG-NAG-BMA
ACT
Metals
_CL ×3
Waters ×124
HEADER    HYDROLASE/HORMONE                       03-APR-12   4APJ
TITLE     HUMAN ANGIOTENSIN-CONVERTING ENZYME IN COMPLEX WITH BPPB
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 68-656;
COMPND   5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143,
COMPND   6  ACE-T;
COMPND   7 EC: 3.2.1.-, 3.4.15.1;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: BRADYKININ-POTENTIATING PEPTIDE B;
COMPND  11 CHAIN: P;
COMPND  12 SYNONYM: POTENTIATOR B
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE   8 MOL_ID: 2;
SOURCE   9 SYNTHETIC: YES;
SOURCE  10 ORGANISM_SCIENTIFIC: GLOYDIUS BLOMHOFFI;
SOURCE  11 ORGANISM_COMMON: MAMUSHI;
SOURCE  12 ORGANISM_TAXID: 242054
KEYWDS    HYDROLASE-HORMONE COMPLEX, ZINC METALLOPROTEASE, METALLOPEPTIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.MASUYER,S.L.U.SCHWAGER,E.D.STURROCK,R.E.ISAAC,K.R.ACHARYA
REVDAT   2   24-OCT-12 4APJ    1       JRNL
REVDAT   1   17-OCT-12 4APJ    0
JRNL        AUTH   G.MASUYER,S.L.U.SCHWAGER,E.D.STURROCK,R.E.ISAAC,K.R.ACHARYA
JRNL        TITL   MOLECULAR RECOGNITION AND REGULATION OF HUMAN ANGIOTENSIN-I
JRNL        TITL 2 CONVERTING ENZYME (ACE) ACTIVITY BY NATURAL INHIBITORY
JRNL        TITL 3 PEPTIDES.
JRNL        REF    SCI.REP.                      V.   2   717 2012
JRNL        REFN                   ISSN 2045-2322
JRNL        PMID   23056909
JRNL        DOI    10.1038/SREP00717
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.82
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.91
REMARK   3   NUMBER OF REFLECTIONS             : 18936
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) : 0.21723
REMARK   3   R VALUE            (WORKING SET) : 0.21518
REMARK   3   FREE R VALUE                     : 0.25611
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1
REMARK   3   FREE R VALUE TEST SET COUNT      : 1028
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.600
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.667
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1345
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.32
REMARK   3   BIN R VALUE           (WORKING SET) : 0.237
REMARK   3   BIN FREE R VALUE SET COUNT          : 93
REMARK   3   BIN FREE R VALUE                    : 0.318
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4835
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 107
REMARK   3   SOLVENT ATOMS            : 124
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.597
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.67
REMARK   3    B22 (A**2) : -0.16
REMARK   3    B33 (A**2) : 0.84
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): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.354
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.248
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.515
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.908
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.868
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5085 ; 0.006 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6905 ; 0.976 ; 1.959
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   591 ; 4.823 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   250 ;34.841 ;24.240
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   823 ;14.494 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;14.152 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   724 ; 0.066 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3899 ; 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):  2976 ; 0.268 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4809 ; 0.520 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2109 ; 0.632 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2096 ; 1.136 ; 4.500
REMARK   3
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    40        A   624
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3897  -6.0983 -23.4708
REMARK   3    T TENSOR
REMARK   3      T11:   0.0109 T22:   0.0202
REMARK   3      T33:   0.0342 T12:   0.0039
REMARK   3      T13:   0.0013 T23:   0.0144
REMARK   3    L TENSOR
REMARK   3      L11:   0.2220 L22:   0.6610
REMARK   3      L33:   0.6691 L12:  -0.1141
REMARK   3      L13:  -0.0396 L23:   0.4899
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0083 S12:  -0.0053 S13:  -0.0131
REMARK   3      S21:   0.0539 S22:   0.0411 S23:  -0.0647
REMARK   3      S31:   0.0351 S32:   0.0351 S33:  -0.0327
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.
REMARK   4
REMARK   4 4APJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-12.
REMARK 100 THE PDBE ID CODE IS EBI-51980.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-12
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : DIAMOND
REMARK 200  BEAMLINE                       : I04
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS-2M)
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20038
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.60
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.82
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7
REMARK 200  DATA REDUNDANCY                : 4.8
REMARK 200  R MERGE                    (I) : 0.13
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.7
REMARK 200  R MERGE FOR SHELL          (I) : 0.48
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.50
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 1O8A
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM SODIUM ACETATE PH 4.7, 15%
REMARK 280  PEG4000, 10UM ZNSO4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-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       28.43500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.61000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.64000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.61000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.43500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.64000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     LEU A    37
REMARK 465     VAL A    38
REMARK 465     THR A    39
REMARK 465     SER A   435
REMARK 465     GLU A   436
REMARK 465     GLY A   437
REMARK 465     GLY A   438
REMARK 465     SER A   625
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  72       79.78   -158.05
REMARK 500    GLU A 123     -133.13     59.16
REMARK 500    ARG A 348     -154.31    -74.96
REMARK 500    GLU A 349       80.45     55.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     PE4 A 1629
REMARK 610     PE4 A 1630
REMARK 610     PE4 A 1631
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A1629
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A1630
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A1631
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1635
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800   ASN A 109 RESIDUES 1632 TO 1634
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O86   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERING ENZYME
REMARK 900  IN COMPLEX WITH LISINOPRIL.
REMARK 900 RELATED ID: 1O8A   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERING ENZYME (
REMARK 900  NATIVE).
REMARK 900 RELATED ID: 1UZE   RELATED DB: PDB
REMARK 900  COMPLEX OF THE ANTI-HYPERTENSIVE DRUG ENALAPRIL AN THE
REMARK 900   HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME
REMARK 900 RELATED ID: 1UZF   RELATED DB: PDB
REMARK 900  COMPLEX OF THE ANTI-HYPERTENSIVE DRUG CAPTOPRIL AN THE
REMARK 900   HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME
REMARK 900 RELATED ID: 2C6F   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING
REMARK 900  ENZYME N DOMAIN
REMARK 900 RELATED ID: 2C6N   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING
REMARK 900  ENZYME N DOMAIN WITH LISINOPRIL
REMARK 900 RELATED ID: 2IUL   RELATED DB: PDB
REMARK 900  HUMAN TACE G13 MUTANT
REMARK 900 RELATED ID: 2IUX   RELATED DB: PDB
REMARK 900  HUMAN TACE MUTANT G1234
REMARK 900 RELATED ID: 2XY9   RELATED DB: PDB
REMARK 900  HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH
REMARK 900  PHOSPHINIC TRIPEPTIDE
REMARK 900 RELATED ID: 2XYD   RELATED DB: PDB
REMARK 900  HUMAN ANGIOTENISN CONVERTING ENZYME N-DOMAIN IN COMPLEX
REMARK 900   WITH PHOSPHINIC TRIPEPTIDE
REMARK 900 RELATED ID: 2YDM   RELATED DB: PDB
REMARK 900  STRUCTURAL CHARACTERIZATION OF ANGIOTENSIN-I CONVERTING
REMARK 900  ENZYME IN COMPLEX WITH A SELENIUM ANALOGUE OF
REMARK 900  CAPTOPRIL
REMARK 900 RELATED ID: 4APH   RELATED DB: PDB
REMARK 900  HUMAN ANGIOTENSIN-CONVERTING ENZYME IN COMPLEX WITH
REMARK 900  ANGIOTENSIN-II
DBREF  4APJ A   37   625  UNP    P12821   ACE_HUMAN       68    656
DBREF  4APJ P    1    11  UNP    P01021   BNP_GLOBL       85     95
SEQRES   1 A  589  LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL GLU
SEQRES   2 A  589  GLU TYR ASP ARG THR SER GLN VAL VAL TRP ASN GLU TYR
SEQRES   3 A  589  ALA GLU ALA ASN TRP ASN TYR ASN THR ASN ILE THR THR
SEQRES   4 A  589  GLU THR SER LYS ILE LEU LEU GLN LYS ASN MET GLN ILE
SEQRES   5 A  589  ALA ASN HIS THR LEU LYS TYR GLY THR GLN ALA ARG LYS
SEQRES   6 A  589  PHE ASP VAL ASN GLN LEU GLN ASN THR THR ILE LYS ARG
SEQRES   7 A  589  ILE ILE LYS LYS VAL GLN ASP LEU GLU ARG ALA ALA LEU
SEQRES   8 A  589  PRO ALA GLN GLU LEU GLU GLU TYR ASN LYS ILE LEU LEU
SEQRES   9 A  589  ASP MET GLU THR THR TYR SER VAL ALA THR VAL CYS HIS
SEQRES  10 A  589  PRO ASN GLY SER CYS LEU GLN LEU GLU PRO ASP LEU THR
SEQRES  11 A  589  ASN VAL MET ALA THR SER ARG LYS TYR GLU ASP LEU LEU
SEQRES  12 A  589  TRP ALA TRP GLU GLY TRP ARG ASP LYS ALA GLY ARG ALA
SEQRES  13 A  589  ILE LEU GLN PHE TYR PRO LYS TYR VAL GLU LEU ILE ASN
SEQRES  14 A  589  GLN ALA ALA ARG LEU ASN GLY TYR VAL ASP ALA GLY ASP
SEQRES  15 A  589  SER TRP ARG SER MET TYR GLU THR PRO SER LEU GLU GLN
SEQRES  16 A  589  ASP LEU GLU ARG LEU PHE GLN GLU LEU GLN PRO LEU TYR
SEQRES  17 A  589  LEU ASN LEU HIS ALA TYR VAL ARG ARG ALA LEU HIS ARG
SEQRES  18 A  589  HIS TYR GLY ALA GLN HIS ILE ASN LEU GLU GLY PRO ILE
SEQRES  19 A  589  PRO ALA HIS LEU LEU GLY ASN MET TRP ALA GLN THR TRP
SEQRES  20 A  589  SER ASN ILE TYR ASP LEU VAL VAL PRO PHE PRO SER ALA
SEQRES  21 A  589  PRO SER MET ASP THR THR GLU ALA MET LEU LYS GLN GLY
SEQRES  22 A  589  TRP THR PRO ARG ARG MET PHE LYS GLU ALA ASP ASP PHE
SEQRES  23 A  589  PHE THR SER LEU GLY LEU LEU PRO VAL PRO PRO GLU PHE
SEQRES  24 A  589  TRP ASN LYS SER MET LEU GLU LYS PRO THR ASP GLY ARG
SEQRES  25 A  589  GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR ASN
SEQRES  26 A  589  GLY LYS ASP PHE ARG ILE LYS GLN CYS THR THR VAL ASN
SEQRES  27 A  589  LEU GLU ASP LEU VAL VAL ALA HIS HIS GLU MET GLY HIS
SEQRES  28 A  589  ILE GLN TYR PHE MET GLN TYR LYS ASP LEU PRO VAL ALA
SEQRES  29 A  589  LEU ARG GLU GLY ALA ASN PRO GLY PHE HIS GLU ALA ILE
SEQRES  30 A  589  GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO LYS HIS
SEQRES  31 A  589  LEU HIS SER LEU ASN LEU LEU SER SER GLU GLY GLY SER
SEQRES  32 A  589  ASP GLU HIS ASP ILE ASN PHE LEU MET LYS MET ALA LEU
SEQRES  33 A  589  ASP LYS ILE ALA PHE ILE PRO PHE SER TYR LEU VAL ASP
SEQRES  34 A  589  GLN TRP ARG TRP ARG VAL PHE ASP GLY SER ILE THR LYS
SEQRES  35 A  589  GLU ASN TYR ASN GLN GLU TRP TRP SER LEU ARG LEU LYS
SEQRES  36 A  589  TYR GLN GLY LEU CYS PRO PRO VAL PRO ARG THR GLN GLY
SEQRES  37 A  589  ASP PHE ASP PRO GLY ALA LYS PHE HIS ILE PRO SER SER
SEQRES  38 A  589  VAL PRO TYR ILE ARG TYR PHE VAL SER PHE ILE ILE GLN
SEQRES  39 A  589  PHE GLN PHE HIS GLU ALA LEU CYS GLN ALA ALA GLY HIS
SEQRES  40 A  589  THR GLY PRO LEU HIS LYS CYS ASP ILE TYR GLN SER LYS
SEQRES  41 A  589  GLU ALA GLY GLN ARG LEU ALA THR ALA MET LYS LEU GLY
SEQRES  42 A  589  PHE SER ARG PRO TRP PRO GLU ALA MET GLN LEU ILE THR
SEQRES  43 A  589  GLY GLN PRO ASN MET SER ALA SER ALA MET LEU SER TYR
SEQRES  44 A  589  PHE LYS PRO LEU LEU ASP TRP LEU ARG THR GLU ASN GLU
SEQRES  45 A  589  LEU HIS GLY GLU LYS LEU GLY TRP PRO GLN TYR ASN TRP
SEQRES  46 A  589  THR PRO ASN SER
SEQRES   1 P   11  PCA GLY LEU PRO PRO ARG PRO LYS ILE PRO PRO
MODRES 4APJ PCA P    1  GLN  PYROGLUTAMIC ACID
HET    PCA  P   1       8
HET     CL  A1625       1
HET    SO4  A1626       5
HET     CL  A1627       1
HET     CL  A1628       1
HET    PE4  A1629      16
HET    PE4  A1630      16
HET    PE4  A1631      16
HET    NAG  A1632      14
HET    NAG  A1633      14
HET    BMA  A1634      11
HET    ACT  A1635       4
HETNAM     PCA PYROGLUTAMIC ACID
HETNAM      CL CHLORIDE ION
HETNAM     SO4 SULFATE ION
HETNAM     PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM   2 PE4  ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     ACT ACETATE ION
HETSYN     PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL   2  PCA    C5 H7 N O3
FORMUL   3   CL    3(CL 1-)
FORMUL   4  SO4    O4 S 2-
FORMUL   5  PE4    3(C16 H34 O8)
FORMUL   6  NAG    2(C8 H15 N O6)
FORMUL   7  BMA    C6 H12 O6
FORMUL   8  ACT    C2 H3 O2 1-
FORMUL   9  HOH   *124(H2 O)
HELIX    1   1 ASP A   40  ASN A   72  1                                  33
HELIX    2   2 THR A   74  ARG A  100  1                                  27
HELIX    3   3 ASP A  103  LEU A  107  5                                   5
HELIX    4   4 ASN A  109  GLN A  120  1                                  12
HELIX    5   5 LEU A  122  LEU A  127  5                                   6
HELIX    6   6 PRO A  128  ALA A  149  1                                  22
HELIX    7   7 PRO A  163  SER A  172  1                                  10
HELIX    8   8 LYS A  174  LEU A  194  1                                  21
HELIX    9   9 PHE A  196  LEU A  210  1                                  15
HELIX   10  10 ASP A  215  SER A  222  1                                   8
HELIX   11  11 MET A  223  GLU A  225  5                                   3
HELIX   12  12 SER A  228  LEU A  240  1                                  13
HELIX   13  13 LEU A  240  GLY A  260  1                                  21
HELIX   14  14 TRP A  283  ASN A  285  5                                   3
HELIX   15  15 ILE A  286  VAL A  291  1                                   6
HELIX   16  16 ASP A  300  GLN A  308  1                                   9
HELIX   17  17 THR A  311  LEU A  326  1                                  16
HELIX   18  18 PRO A  332  SER A  339  1                                   8
HELIX   19  19 ASN A  374  TYR A  394  1                                  21
HELIX   20  20 PRO A  398  ARG A  402  5                                   5
HELIX   21  21 ASN A  406  THR A  423  1                                  18
HELIX   22  22 THR A  423  LEU A  430  1                                   8
HELIX   23  23 SER A  439  ILE A  455  1                                  17
HELIX   24  24 ALA A  456  ASP A  473  1                                  18
HELIX   25  25 ASN A  480  GLY A  494  1                                  15
HELIX   26  26 PHE A  506  LYS A  511  5                                   6
HELIX   27  27 TYR A  520  ALA A  541  1                                  22
HELIX   28  28 PRO A  546  CYS A  550  5                                   5
HELIX   29  29 SER A  555  LEU A  568  1                                  14
HELIX   30  30 PRO A  573  GLY A  583  1                                  11
HELIX   31  31 ALA A  589  PHE A  596  1                                   8
HELIX   32  32 PHE A  596  GLY A  611  1                                  16
SHEET    1  AA 2 THR A 150  CYS A 152  0
SHEET    2  AA 2 CYS A 158  GLN A 160 -1  O  LEU A 159   N  VAL A 151
SHEET    1  AB 2 ILE A 270  PRO A 271  0
SHEET    2  AB 2 LEU A 495  CYS A 496  1  N  CYS A 496   O  ILE A 270
SHEET    1  AC 2 SER A 355  ASP A 358  0
SHEET    2  AC 2 PHE A 365  LYS A 368 -1  O  ARG A 366   N  TRP A 357
SSBOND   1 CYS A  152    CYS A  158                          1555   1555  2.04
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.04
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.03
LINK         ND2 ASN A 109                 C1  NAG A1632     1555   1555  1.44
LINK         O4  NAG A1632                 C1  NAG A1633     1555   1555  1.44
LINK         C1  BMA A1634                 O4  NAG A1633     1555   1555  1.45
LINK         C   PCA P   1                 N   GLY P   2     1555   1555  1.33
CISPEP   1 GLU A  162    PRO A  163          0         2.08
SITE     1 AC1  5 ARG A 186  TRP A 485  TRP A 486  ARG A 489
SITE     2 AC1  5 HOH A2037
SITE     1 AC2  2 SER A 298  LEU A 580
SITE     1 AC3  1 ARG A 522
SITE     1 AC4  4 TYR A 224  PRO A 407  PRO A 519  ARG A 522
SITE     1 AC5  2 SER A 284  LYS A 449
SITE     1 AC6  6 ASN A 205  THR A 324  GLY A 327  PHE A 472
SITE     2 AC6  6 GLN A 554  LYS A 556
SITE     1 AC7  9 LYS A  46  TYR A 250  ARG A 253  ALA A 254
SITE     2 AC7  9 ARG A 257  VAL A 290  VAL A 291  PRO A 292
SITE     3 AC7  9 HIS A 610
SITE     1 AC8  4 HIS A 383  GLU A 411  ASP A 415  PRO P  11
SITE     1 AC9  3 GLU A  43  ASN A 109  HOH A2121
CRYST1   56.870   85.280  133.220  90.00  90.00  90.00 P 21 21 21    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      0.017584  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011726  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007506        0.00000
      
PROCHECK
Go to PROCHECK summary
 References