HEADER HYDROLASE 07-OCT-13 4CA5
TITLE HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH A PHOSPHINIC
TITLE 2 TRIPEPTIDE FI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 68-656;
COMPND 5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143,
COMPND 6 ANGIOTENSIN-CONVERTING ENZYME, SOLUBLE FORM;
COMPND 7 EC: 3.2.1.-, 3.4.15.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: TESTIS;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: CHO
KEYWDS HYDROLASE, ZINC METALLOPEPTIDASE, INHIBITOR BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MASUYER,M.AKIF,B.CZARNY,F.BEAU,S.L.U.SCHWAGER,E.D.STURROCK,
AUTHOR 2 R.E.ISAAC,V.DIVE,K.R.ACHARYA
REVDAT 4 20-DEC-23 4CA5 1 HETSYN
REVDAT 3 29-JUL-20 4CA5 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 12-FEB-14 4CA5 1 JRNL
REVDAT 1 11-DEC-13 4CA5 0
JRNL AUTH G.MASUYER,M.AKIF,B.CZARNY,F.BEAU,S.L.SCHWAGER,E.D.STURROCK,
JRNL AUTH 2 R.E.ISAAC,V.DIVE,K.R.ACHARYA
JRNL TITL CRYSTAL STRUCTURES OF HIGHLY SPECIFIC PHOSPHINIC TRIPEPTIDE
JRNL TITL 2 ENANTIOMERS IN COMPLEX WITH THE ANGIOTENSIN-I CONVERTING
JRNL TITL 3 ENZYME.
JRNL REF FEBS J. V. 281 943 2014
JRNL REFN ISSN 1742-464X
JRNL PMID 24289879
JRNL DOI 10.1111/FEBS.12660
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
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) : 71.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 49962
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2668
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3557
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 204
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4778
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 125
REMARK 3 SOLVENT ATOMS : 379
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.49000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.47000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.149
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.078
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5079 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6913 ; 1.216 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 591 ; 5.284 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 251 ;36.948 ;24.303
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 817 ;13.830 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;20.059 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 725 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3948 ; 0.006 ; 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): 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : 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 1632
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3105 -5.3188 -23.8359
REMARK 3 T TENSOR
REMARK 3 T11: 0.0104 T22: 0.0044
REMARK 3 T33: 0.0060 T12: 0.0029
REMARK 3 T13: 0.0028 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.1625 L22: 0.3532
REMARK 3 L33: 0.4262 L12: -0.0181
REMARK 3 L13: -0.0343 L23: 0.1786
REMARK 3 S TENSOR
REMARK 3 S11: -0.0128 S12: -0.0237 S13: -0.0156
REMARK 3 S21: 0.0188 S22: 0.0108 S23: -0.0191
REMARK 3 S31: 0.0026 S32: 0.0072 S33: 0.0019
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4CA5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1290058644.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
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) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52682
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 71.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
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) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.42000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 2XY9
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MIB PH4.0, 10UM ZINC SULPHATE, 5%
REMARK 280 GLYCEROL, 15% PEG3350
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 28.21500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.95000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.49000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.95000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.21500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.49000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 LEU A 37
REMARK 465 VAL A 38
REMARK 465 THR A 39
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 ND2 ASN A 624 O HOH A 2376 1.94
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 72 77.84 -175.66
REMARK 500 GLN A 108 -71.13 -65.06
REMARK 500 GLU A 123 -137.93 53.21
REMARK 500 ALA A 296 74.70 -113.42
REMARK 500 ASP A 346 -15.24 -49.39
REMARK 500 SER A 439 112.53 -27.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 5,6-DIHYDRO-BENZO[H]CINNOLIN-3-YLAMINE (3EF): ENANTIOMER TO
REMARK 600 MOLECULE 3ES SEEN IN PDB 2XY9
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 A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 383 NE2
REMARK 620 2 HIS A 387 NE2 109.6
REMARK 620 3 GLU A 411 OE1 91.7 100.8
REMARK 620 4 3EF A1700 OAG 96.9 88.5 164.4
REMARK 620 5 3EF A1700 OAD 108.2 136.1 99.7 65.3
REMARK 620 N 1 2 3 4
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: N-{(2S)-3-[(S)-[(1R)-1-{[(BENZYLOXY)CARBONYL]AMINO}-
REMARK 630 2-PHENYLETHYL](HYDROXY)PHOSPHORYL]-2-[(3-PHENYL-1,2-OXAZOL-5-YL)
REMARK 630 METHYL]PROPANOYL}-L-TYROSINE
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 3EF A 1700
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: PHQ PPH 1JK TYR
REMARK 630 DETAILS: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CA6 RELATED DB: PDB
REMARK 900 HUMAN ANGIOTENSIN CONVERTING ENZYME N-DOMAIN IN COMPLEX WITH A
REMARK 900 PHOSPHINIC TRIPEPTIDE FI
REMARK 900 RELATED ID: 4CA7 RELATED DB: PDB
REMARK 900 DROSOPHILA ANGIOTENSIN CONVERTING ENZYME (ANCE) IN COMPLEX WITH A
REMARK 900 PHOSPHINIC TRIPEPTIDE FI
REMARK 900 RELATED ID: 4CA8 RELATED DB: PDB
REMARK 900 DROSOPHILA ANGIOTENSIN CONVERTING ENZYME (ANCE) IN COMPLEX WITH A
REMARK 900 PHOSPHINIC TRIPEPTIDE FII
DBREF 4CA5 A 37 625 UNP P12821 ACE_HUMAN 68 656
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
MODRES 4CA5 ASN A 72 ASN GLYCOSYLATION SITE
MODRES 4CA5 ASN A 109 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET FUC B 3 10
HET ZN A1001 1
HET CL A1002 1
HET CL A1003 1
HET ACT A1100 4
HET ACT A1101 4
HET ACT A1102 4
HET PEG A1103 7
HET 3EF A1700 51
HET NAG A1632 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 3EF N-{(2S)-3-[(S)-[(1R)-1-{[(BENZYLOXY)CARBONYL]AMINO}-2-
HETNAM 2 3EF PHENYLETHYL](HYDROXY)PHOSPHORYL]-2-[(3-PHENYL-1,2-
HETNAM 3 3EF OXAZOL-5-YL)METHYL]PROPANOYL}-L-TYROSINE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 2 FUC C6 H12 O5
FORMUL 3 ZN ZN 2+
FORMUL 4 CL 2(CL 1-)
FORMUL 6 ACT 3(C2 H3 O2 1-)
FORMUL 9 PEG C4 H10 O3
FORMUL 10 3EF C38 H38 N3 O9 P
FORMUL 12 HOH *379(H2 O)
HELIX 1 1 ASP A 40 THR A 71 1 32
HELIX 2 2 THR A 74 LYS A 101 1 28
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 ALA A 189 1 16
HELIX 9 9 ALA A 189 LEU A 194 1 6
HELIX 10 10 PHE A 196 ASN A 211 1 16
HELIX 11 11 ASP A 215 SER A 222 1 8
HELIX 12 12 MET A 223 GLU A 225 5 3
HELIX 13 13 SER A 228 LEU A 240 1 13
HELIX 14 14 LEU A 240 GLY A 260 1 21
HELIX 15 15 TRP A 283 ASN A 285 5 3
HELIX 16 16 ILE A 286 VAL A 291 1 6
HELIX 17 17 ASP A 300 GLN A 308 1 9
HELIX 18 18 THR A 311 LEU A 326 1 16
HELIX 19 19 PRO A 332 SER A 339 1 8
HELIX 20 20 ASN A 374 TYR A 394 1 21
HELIX 21 21 PRO A 398 ARG A 402 5 5
HELIX 22 22 ASN A 406 SER A 422 1 17
HELIX 23 23 THR A 423 LEU A 430 1 8
HELIX 24 24 SER A 439 ILE A 455 1 17
HELIX 25 25 ALA A 456 ASP A 473 1 18
HELIX 26 26 ASN A 480 GLY A 494 1 15
HELIX 27 27 PHE A 506 LYS A 511 5 6
HELIX 28 28 TYR A 520 ALA A 541 1 22
HELIX 29 29 PRO A 546 CYS A 550 5 5
HELIX 30 30 SER A 555 LEU A 568 1 14
HELIX 31 31 PRO A 573 GLY A 583 1 11
HELIX 32 32 ALA A 589 HIS A 610 1 22
SHEET 1 AA 2 VAL A 151 CYS A 152 0
SHEET 2 AA 2 CYS A 158 LEU A 159 -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 2.03
SSBOND 2 CYS A 352 CYS A 370 1555 1555 2.02
SSBOND 3 CYS A 538 CYS A 550 1555 1555 2.03
LINK ND2 ASN A 72 C1 NAG A1632 1555 1555 1.44
LINK ND2 ASN A 109 C1 NAG B 1 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O6 NAG B 1 C1 FUC B 3 1555 1555 1.44
LINK NE2 HIS A 383 ZN ZN A1001 1555 1555 2.08
LINK NE2 HIS A 387 ZN ZN A1001 1555 1555 2.04
LINK OE1 GLU A 411 ZN ZN A1001 1555 1555 1.97
LINK ZN ZN A1001 OAG 3EF A1700 1555 1555 2.42
LINK ZN ZN A1001 OAD 3EF A1700 1555 1555 2.24
CISPEP 1 GLU A 162 PRO A 163 0 8.05
CRYST1 56.430 84.980 133.900 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 0.017721 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011767 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007468 0.00000
(ATOM LINES ARE NOT SHOWN.)
END