HEADER HYDROLASE 22-MAR-11 2YDM
TITLE STRUCTURAL CHARACTERIZATION OF ANGIOTENSIN-I CONVERTING ENZYME IN
TITLE 2 COMPLEX WITH A SELENIUM ANALOGUE OF CAPTOPRIL
CAVEAT 2YDM SLC A 1626 HAS WRONG CHIRALITY AT ATOM C8
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: DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143;
COMPND 6 EC: 3.4.15.1;
COMPND 7 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: TESTES;
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;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PLEN
KEYWDS HYDROLASE, ANTIHYPERTENSIVE AGENTS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.AKIF,G.MASUYER,S.L.U.SCHWAGER,B.J.BHUYAN,G.MUGESH,E.D.STURROCK,
AUTHOR 2 K.R.ACHARYA
REVDAT 5 20-DEC-23 2YDM 1 HETSYN
REVDAT 4 29-JUL-20 2YDM 1 CAVEAT COMPND REMARK HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 21-NOV-12 2YDM 1 DBREF
REVDAT 2 19-OCT-11 2YDM 1 JRNL
REVDAT 1 14-SEP-11 2YDM 0
JRNL AUTH M.AKIF,G.MASUYER,S.L.U.SCHWAGER,B.J.BHUYAN,G.MUGESH,
JRNL AUTH 2 R.E.ISAAC,E.D.STURROCK,K.R.ACHARYA
JRNL TITL STRUCTURAL CHARACTERIZATION OF ANGIOTENSIN-I CONVERTING
JRNL TITL 2 ENZYME IN COMPLEX WITH A SELENIUM ANALOGUE OF CAPTOPRIL
JRNL REF FEBS J. V. 278 3644 2011
JRNL REFN ISSN 1742-464X
JRNL PMID 21810173
JRNL DOI 10.1111/J.1742-4658.2011.08276.X
REMARK 2
REMARK 2 RESOLUTION. 2.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 132.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 22384
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1211
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) : 2.44
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1112
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4687
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 54
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 0.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.11000
REMARK 3 B22 (A**2) : -1.44000
REMARK 3 B33 (A**2) : 3.54000
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): 0.664
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.305
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.000
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.000
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4897 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6661 ; 1.420 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 572 ; 9.457 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 243 ;35.797 ;24.239
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 804 ;15.578 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;19.989 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 707 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3778 ; 0.008 ; 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): 2875 ; 0.531 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4640 ; 1.056 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2022 ; 1.784 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2021 ; 2.967 ; 4.500
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 : 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 RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2YDM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1290047780.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-11
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 : I02
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23627
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 132.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.62000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE, 10UM ZINC
REMARK 280 SULPHATE, 15% PEG4000, PH 4.7
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 28.07150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.13500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.26650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.13500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.07150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.26650
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 465 SER A 435
REMARK 465 GLU A 436
REMARK 465 GLY A 437
REMARK 465 GLY A 438
REMARK 465 TYR A 619
REMARK 465 ASN A 620
REMARK 465 TRP A 621
REMARK 465 THR A 622
REMARK 465 PRO A 623
REMARK 465 ASN A 624
REMARK 465 SER A 625
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 GLN A 618 CA C O CB CG CD OE1
REMARK 470 GLN A 618 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 NH1 ARG A 348 C7 NAG A 1622 1.95
REMARK 500 ND2 ASN A 72 C2 NAG A 1622 2.10
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 68.23 -168.57
REMARK 500 GLU A 123 -138.19 56.38
REMARK 500 ALA A 272 -8.38 -59.46
REMARK 500 ALA A 296 79.83 -119.55
REMARK 500 ASP A 346 -18.42 -43.83
REMARK 500 LYS A 478 -8.60 -57.62
REMARK 500 ARG A 522 -36.83 -37.49
REMARK 500 GLN A 554 -1.53 74.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 SELENO-CAPTOPRIL (SLC): SELENIUM DERIVATIVE OF CAPTOPRIL
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 A1619 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 383 NE2
REMARK 620 2 HIS A 387 NE2 111.4
REMARK 620 3 GLU A 411 OE1 86.7 100.6
REMARK 620 4 SLC A1626 SE 122.0 111.0 121.6
REMARK 620 N 1 2 3
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: SELENO-CAPTOPRIL
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 SLC A 1626
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: CC4 PRO
REMARK 630 DETAILS: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
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: 1UZE RELATED DB: PDB
REMARK 900 COMPLEX OF THE ANTI-HYPERTENSIVE DRUG ENALAPRIL AN THE HUMAN
REMARK 900 TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME
REMARK 900 RELATED ID: 2C6F RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN
REMARK 900 RELATED ID: 1UZF RELATED DB: PDB
REMARK 900 COMPLEX OF THE ANTI-HYPERTENSIVE DRUG CAPTOPRIL AN THE HUMAN
REMARK 900 TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME
REMARK 900 RELATED ID: 1O8A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERING ENZYME (NATIVE).
REMARK 900 RELATED ID: 2XYD RELATED DB: PDB
REMARK 900 HUMAN ANGIOTENISN CONVERTING ENZYME N-DOMAIN IN COMPLEX WITH
REMARK 900 PHOSPHINIC TRIPEPTIDE
REMARK 900 RELATED ID: 2XY9 RELATED DB: PDB
REMARK 900 HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH PHOSPHINIC
REMARK 900 TRIPEPTIDE
REMARK 900 RELATED ID: 2C6N RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N
REMARK 900 DOMAIN WITH LISINOPRIL
REMARK 900 RELATED ID: 1O86 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERING ENZYME IN COMPLEX
REMARK 900 WITH LISINOPRIL.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 UNDERGLYCOSYLATED HUMAN TESTIS ACE VARIANT
DBREF 2YDM A 37 625 UNP P12821 ACE_HUMAN 68 656
SEQADV 2YDM TRP A 616 UNP P12821 PRO 648 CONFLICT
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 GLN GLN TYR ASN TRP
SEQRES 46 A 589 THR PRO ASN SER
MODRES 2YDM ASN A 72 ASN GLYCOSYLATION SITE
MODRES 2YDM ASN A 109 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET ZN A1619 1
HET CL A1620 1
HET CL A1621 1
HET NAG A1622 14
HET SLC A1626 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM SLC SELENO-CAPTOPRIL
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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN SLC 1-[2-(SELANYLMETHYL)ACRYLOYL]-L-PROLINE
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 3 ZN ZN 2+
FORMUL 4 CL 2(CL 1-)
FORMUL 7 SLC C9 H13 N O3 SE
FORMUL 8 HOH *54(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 GLN A 195 1 22
HELIX 9 9 PHE A 196 ASN A 211 1 16
HELIX 10 10 ASP A 215 MET A 223 1 9
HELIX 11 11 SER A 228 LEU A 240 1 13
HELIX 12 12 LEU A 240 GLY A 260 1 21
HELIX 13 13 TRP A 283 ASN A 285 5 3
HELIX 14 14 ILE A 286 VAL A 291 1 6
HELIX 15 15 ASP A 300 GLN A 308 1 9
HELIX 16 16 THR A 311 LEU A 326 1 16
HELIX 17 17 PRO A 332 SER A 339 1 8
HELIX 18 18 ASN A 374 TYR A 394 1 21
HELIX 19 19 PRO A 398 ARG A 402 5 5
HELIX 20 20 ASN A 406 SER A 422 1 17
HELIX 21 21 THR A 423 LEU A 430 1 8
HELIX 22 22 SER A 439 ILE A 455 1 17
HELIX 23 23 ALA A 456 ASP A 473 1 18
HELIX 24 24 ASN A 480 TYR A 492 1 13
HELIX 25 25 PHE A 506 LYS A 511 5 6
HELIX 26 26 TYR A 520 ALA A 541 1 22
HELIX 27 27 PRO A 546 CYS A 550 5 5
HELIX 28 28 SER A 555 LEU A 568 1 14
HELIX 29 29 PRO A 573 GLY A 583 1 11
HELIX 30 30 ALA A 589 PHE A 596 1 8
HELIX 31 31 PHE A 596 HIS A 610 1 15
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 2.06
SSBOND 2 CYS A 352 CYS A 370 1555 1555 2.10
SSBOND 3 CYS A 538 CYS A 550 1555 1555 2.42
LINK ND2 ASN A 72 C1 NAG A1622 1555 1555 1.44
LINK ND2 ASN A 109 C1 NAG B 1 1555 1555 1.44
LINK NH1 ARG A 348 C8 NAG A1622 1555 1555 1.42
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.46
LINK NE2 HIS A 383 ZN ZN A1619 1555 1555 2.01
LINK NE2 HIS A 387 ZN ZN A1619 1555 1555 2.12
LINK OE1 GLU A 411 ZN ZN A1619 1555 1555 1.94
LINK ZN ZN A1619 SE SLC A1626 1555 1555 2.48
CISPEP 1 GLU A 162 PRO A 163 0 -2.10
CRYST1 56.143 84.533 132.270 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 0.017812 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011830 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007560 0.00000
(ATOM LINES ARE NOT SHOWN.)
END