HEADER HYDROLASE 14-MAR-10 2X96
TITLE CRYSTAL STRUCTURE OF ANCE-RXPA380 COMPLEX
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 4 18-APR-12 2X96 1 REMARK VERSN
REVDAT 3 16-MAR-11 2X96 1 REMARK HETSYN
REVDAT 2 21-JUL-10 2X96 1 JRNL ATOM
REVDAT 1 02-JUN-10 2X96 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. 1.85 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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.14
REMARK 3 NUMBER OF REFLECTIONS : 83797
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) : 0.19503
REMARK 3 R VALUE (WORKING SET) : 0.19397
REMARK 3 FREE R VALUE : 0.21478
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4418
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) : 1.850
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.898
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4358
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.305
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.305
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4891
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 160
REMARK 3 SOLVENT ATOMS : 658
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.78
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.843
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): 0.098
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.109
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.000
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.001
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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.
REMARK 4
REMARK 4 2X96 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-10.
REMARK 100 THE PDBE ID CODE IS EBI-43255.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-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 : I02
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 : 96897
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.85
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 (%) : 91.0
REMARK 200 DATA REDUNDANCY : 2.8
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.5
REMARK 200 R MERGE FOR SHELL (I) : 0.24
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.70
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.66
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 86.53400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.96043
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.86133
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 86.53400
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 49.96043
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.86133
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 86.53400
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 49.96043
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.86133
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 99.92086
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 67.72267
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 99.92086
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 67.72267
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 99.92086
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 67.72267
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 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 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 84.71 -159.31
REMARK 500 ASP A 210 111.01 -160.48
REMARK 500 LEU A 345 -132.76 -107.22
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 A1617 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 371 NE2
REMARK 620 2 HIS A 367 NE2 106.5
REMARK 620 3 GLU A 395 OE1 106.0 96.8
REMARK 620 4 RX3 A1615 O3 130.8 112.8 97.5
REMARK 620 N 1 2 3
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: N-({(1S,2R)-2-[(S)-[(1R)-1-{[(BENZYLOXY)CARBONYL]
REMARK 630 AMINO}-2-PHENYLETHYL](HYDROXY)PHOSPHORYL]CYCLOPENTYL}CARBONYL)
REMARK 630 -L-TRYPTOPHAN
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 RX3 A 1615
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: PHQ PPH IQ0 TRP
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 RX3 A1615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A1616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800 SUGAR BOUND TO ASN A 196 RESIDUES 1618 TO 1625
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J38 RELATED DB: PDB
REMARK 900 RIBONUCLEOTIDE REDUCTASE Y730NO2Y AND Y731A
REMARK 900 MODIFIED R1 SUBUNIT OF E. COLI
REMARK 900 RELATED ID: 1J36 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FIRST PDZ DOMAIN
REMARK 900 OF HUMAN SCRIB1
REMARK 900 RELATED ID: 1J37 RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH
REMARK 900 NOVEL INHIBITORS
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: 2X8Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANCE
REMARK 900 RELATED ID: 2X91 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANCE-LISINOPRIL COMPLEX
REMARK 900 RELATED ID: 2X95 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANCE-LISINOPRIL-
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: 2X93 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANCE-TRANDOLAPRILAT COMPLEX
REMARK 900 RELATED ID: 2X97 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANCE-RXP407 COMPLEX
REMARK 900 RELATED ID: 2X90 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANCE-ENALAPRILAT COMPLEX
DBREF 2X96 A 17 614 UNP Q10714 ACE_DROME 17 614
SEQRES 1 A 598 ALA LEU VAL LYS GLU GLU ILE GLN ALA LYS GLU TYR LEU
SEQRES 2 A 598 GLU ASN LEU ASN LYS GLU LEU ALA LYS ARG THR ASN VAL
SEQRES 3 A 598 GLU THR GLU ALA ALA TRP ALA TYR GLY SER ASN ILE THR
SEQRES 4 A 598 ASP GLU ASN GLU LYS LYS LYS ASN GLU ILE SER ALA GLU
SEQRES 5 A 598 LEU ALA LYS PHE MET LYS GLU VAL ALA SER ASP THR THR
SEQRES 6 A 598 LYS PHE GLN TRP ARG SER TYR GLN SER GLU ASP LEU LYS
SEQRES 7 A 598 ARG GLN PHE LYS ALA LEU THR LYS LEU GLY TYR ALA ALA
SEQRES 8 A 598 LEU PRO GLU ASP ASP TYR ALA GLU LEU LEU ASP THR LEU
SEQRES 9 A 598 SER ALA MET GLU SER ASN PHE ALA LYS VAL LYS VAL CYS
SEQRES 10 A 598 ASP TYR LYS ASP SER THR LYS CYS ASP LEU ALA LEU ASP
SEQRES 11 A 598 PRO GLU ILE GLU GLU VAL ILE SER LYS SER ARG ASP HIS
SEQRES 12 A 598 GLU GLU LEU ALA TYR TYR TRP ARG GLU PHE TYR ASP LYS
SEQRES 13 A 598 ALA GLY THR ALA VAL ARG SER GLN PHE GLU ARG TYR VAL
SEQRES 14 A 598 GLU LEU ASN THR LYS ALA ALA LYS LEU ASN ASN PHE THR
SEQRES 15 A 598 SER GLY ALA GLU ALA TRP LEU ASP GLU TYR GLU ASP ASP
SEQRES 16 A 598 THR PHE GLU GLN GLN LEU GLU ASP ILE PHE ALA ASP ILE
SEQRES 17 A 598 ARG PRO LEU TYR GLN GLN ILE HIS GLY TYR VAL ARG PHE
SEQRES 18 A 598 ARG LEU ARG LYS HIS TYR GLY ASP ALA VAL VAL SER GLU
SEQRES 19 A 598 THR GLY PRO ILE PRO MET HIS LEU LEU GLY ASN MET TRP
SEQRES 20 A 598 ALA GLN GLN TRP SER GLU ILE ALA ASP ILE VAL SER PRO
SEQRES 21 A 598 PHE PRO GLU LYS PRO LEU VAL ASP VAL SER ALA GLU MET
SEQRES 22 A 598 GLU LYS GLN GLY TYR THR PRO LEU LYS MET PHE GLN MET
SEQRES 23 A 598 GLY ASP ASP PHE PHE THR SER MET ASN LEU THR LYS LEU
SEQRES 24 A 598 PRO GLN ASP PHE TRP ASP LYS SER ILE ILE GLU LYS PRO
SEQRES 25 A 598 THR ASP GLY ARG ASP LEU VAL CYS HIS ALA SER ALA TRP
SEQRES 26 A 598 ASP PHE TYR LEU THR ASP ASP VAL ARG ILE LYS GLN CYS
SEQRES 27 A 598 THR ARG VAL THR GLN ASP GLN LEU PHE THR VAL HIS HIS
SEQRES 28 A 598 GLU LEU GLY HIS ILE GLN TYR PHE LEU GLN TYR GLN HIS
SEQRES 29 A 598 GLN PRO PHE VAL TYR ARG THR GLY ALA ASN PRO GLY PHE
SEQRES 30 A 598 HIS GLU ALA VAL GLY ASP VAL LEU SER LEU SER VAL SER
SEQRES 31 A 598 THR PRO LYS HIS LEU GLU LYS ILE GLY LEU LEU LYS ASP
SEQRES 32 A 598 TYR VAL ARG ASP ASP GLU ALA ARG ILE ASN GLN LEU PHE
SEQRES 33 A 598 LEU THR ALA LEU ASP LYS ILE VAL PHE LEU PRO PHE ALA
SEQRES 34 A 598 PHE THR MET ASP LYS TYR ARG TRP SER LEU PHE ARG GLY
SEQRES 35 A 598 GLU VAL ASP LYS ALA ASN TRP ASN CYS ALA PHE TRP LYS
SEQRES 36 A 598 LEU ARG ASP GLU TYR SER GLY ILE GLU PRO PRO VAL VAL
SEQRES 37 A 598 ARG SER GLU LYS ASP PHE ASP ALA PRO ALA LYS TYR HIS
SEQRES 38 A 598 ILE SER ALA ASP VAL GLU TYR LEU ARG TYR LEU VAL SER
SEQRES 39 A 598 PHE ILE ILE GLN PHE GLN PHE TYR LYS SER ALA CYS ILE
SEQRES 40 A 598 LYS ALA GLY GLN TYR ASP PRO ASP ASN VAL GLU LEU PRO
SEQRES 41 A 598 LEU ASP ASN CYS ASP ILE TYR GLY SER ALA ALA ALA GLY
SEQRES 42 A 598 ALA ALA PHE HIS ASN MET LEU SER MET GLY ALA SER LYS
SEQRES 43 A 598 PRO TRP PRO ASP ALA LEU GLU ALA PHE ASN GLY GLU ARG
SEQRES 44 A 598 ILE MET SER GLY LYS ALA ILE ALA GLU TYR PHE GLU PRO
SEQRES 45 A 598 LEU ARG VAL TRP LEU GLU ALA GLU ASN ILE LYS ASN ASN
SEQRES 46 A 598 VAL HIS ILE GLY TRP THR THR SER ASN LYS CYS VAL SER
HET RX3 A1615 44
HET EPE A1616 15
HET ZN A1617 1
HET NAG A1618 14
HET NAG A1619 14
HET BMA A1620 11
HET BMA A1621 11
HET NAG A1623 14
HET NAG A1624 14
HET MAN A1625 11
HET MAN A1622 11
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE
HETNAM 2 EPE ETHANESULFONIC ACID
HETNAM RX3 N-({(1S,2R)-2-[(S)-[(1R)-1-{[(BENZYLOXY)
HETNAM 2 RX3 CARBONYL]AMINO}-2-PHENYLETHYL](HYDROXY)PHOSPHORYL]
HETNAM 3 RX3 CYCLOPENTYL}CARBONYL)-L-TRYPTOPHAN
HETNAM ZN ZINC ION
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN EPE HEPES
HETSYN RX3 RXPA380
FORMUL 2 EPE C8 H18 N2 O4 S
FORMUL 3 RX3 C33 H36 N3 O7 P
FORMUL 4 ZN ZN 2+
FORMUL 5 BMA 2(C6 H12 O6)
FORMUL 5 MAN 2(C6 H12 O6)
FORMUL 6 NAG 4(C8 H15 N O6)
FORMUL 7 HOH *658(H2 O)
HELIX 1 1 ALA A 17 ASN A 53 1 37
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 ILE A 254 PRO A 255 0
SHEET 2 AA 2 ILE A 479 GLU A 480 1 N GLU A 480 O ILE A 254
SHEET 1 AB 2 SER A 339 ASP A 342 0
SHEET 2 AB 2 VAL A 349 LYS A 352 -1 O ARG A 350 N TRP A 341
SHEET 1 AC 2 ARG A 485 SER A 486 0
SHEET 2 AC 2 CYS A 612 VAL A 613 1 N VAL A 613 O ARG A 485
SSBOND 1 CYS A 133 CYS A 141 1555 1555 2.04
SSBOND 2 CYS A 336 CYS A 354 1555 1555 2.05
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 A1624 1555 1555 1.45
LINK ND2 ASN A 196 C1 NAG A1618 1555 1555 1.44
LINK ND2 ASN A 311 C1 NAG A1623 1555 1555 1.44
LINK O3 RX3 A1615 ZN ZN A1617 1555 1555 1.97
LINK ZN ZN A1617 NE2 HIS A 371 1555 1555 2.00
LINK ZN ZN A1617 NE2 HIS A 367 1555 1555 2.10
LINK ZN ZN A1617 OE1 GLU A 395 1555 1555 1.93
LINK O4 NAG A1618 C1 NAG A1619 1555 1555 1.45
LINK O4 NAG A1619 C1 BMA A1620 1555 1555 1.44
LINK O6 BMA A1620 C1 MAN A1622 1555 1555 1.44
LINK O3 BMA A1620 C1 MAN A1625 1555 1555 1.45
LINK C1 BMA A1621 O6 MAN A1625 1555 1555 1.44
CISPEP 1 ASP A 146 PRO A 147 0 4.98
SITE 1 AC1 23 GLN A 266 HIS A 337 ALA A 338 SER A 339
SITE 2 AC1 23 ALA A 340 HIS A 367 GLU A 368 HIS A 371
SITE 3 AC1 23 PHE A 375 HIS A 394 GLU A 395 ASP A 399
SITE 4 AC1 23 PHE A 441 LYS A 495 HIS A 497 VAL A 502
SITE 5 AC1 23 TYR A 504 TYR A 507 EPE A1616 ZN A1617
SITE 6 AC1 23 HOH A2418 HOH A2638 HOH A2639
SITE 1 AC2 7 TYR A 344 THR A 387 ASP A 501 ARG A 506
SITE 2 AC2 7 RX3 A1615 HOH A2546 HOH A2643
SITE 1 AC3 4 HIS A 367 HIS A 371 GLU A 395 RX3 A1615
SITE 1 AC4 24 ASN A 53 THR A 55 ARG A 157 HIS A 159
SITE 2 AC4 24 ASN A 196 ARG A 238 LYS A 241 HIS A 242
SITE 3 AC4 24 TYR A 243 GLY A 244 PRO A 278 ASN A 311
SITE 4 AC4 24 ASP A 330 ARG A 332 HOH A2325 HOH A2644
SITE 5 AC4 24 HOH A2646 HOH A2647 HOH A2649 HOH A2650
SITE 6 AC4 24 HOH A2651 HOH A2653 HOH A2657 HOH A2658
CRYST1 173.068 173.068 101.584 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 0.005778 0.003336 0.000000 0.00000
SCALE2 0.000000 0.006672 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009844 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
