HEADER HYDROLASE 22-SEP-03 1UOQ
TITLE PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND
TITLE 2 PEPTIDE LIGAND GLU-PHE-SER-PRO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: POST-PROLINE CLEAVING ENZYME, PE, PREP;
COMPND 5 EC: 3.4.21.26;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: ENGINEERED MUTATION SER 554 ALA;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PEPTIDE LIGAND GLU-PHE-SER-PRO;
COMPND 11 CHAIN: B;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 TISSUE: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630
KEYWDS HYDROLASE, PROLYL OLIGOPEPTIDASE, AMNESIA, ALPHA/ BETA-HYDROLASE,
KEYWDS 2 BETA-PROPELLER, SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.REA,V.FULOP
REVDAT 5 13-DEC-23 1UOQ 1 REMARK
REVDAT 4 08-FEB-17 1UOQ 1 SOURCE REMARK VERSN HETSYN
REVDAT 4 2 1 FORMUL
REVDAT 3 24-FEB-09 1UOQ 1 VERSN
REVDAT 2 04-DEC-03 1UOQ 1 JRNL
REVDAT 1 02-OCT-03 1UOQ 0
JRNL AUTH Z.SZELTNER,D.REA,V.RENNER,L.JULIANO,V.FULOP,L.POLGAR
JRNL TITL ELECTROSTATIC ENVIRONMENT AT THE ACTIVE SITE OF PROLYL
JRNL TITL 2 OLIGOPEPTIDASE IS HIGHLY INFLUENTIAL DURING SUBSTRATE
JRNL TITL 3 BINDING
JRNL REF J.BIOL.CHEM. V. 278 48786 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 14514675
JRNL DOI 10.1074/JBC.M309555200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.SZELTNER,D.REA,V.RENNER,V.FULOP,L.POLGAR
REMARK 1 TITL ELECTROSTATIC EFFECTS AND BINDING DETERMINANTS IN THE
REMARK 1 TITL 2 CATALYSIS OF PROLYL OLIGOPEPTIDASE: SITE SPECIFIC
REMARK 1 TITL 3 MUTAGENESIS AT THE OXYANION BINDING SITE
REMARK 1 REF J.BIOL.CHEM. V. 277 42613 2002
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 12202494
REMARK 1 DOI 10.1074/JBC.M208043200
REMARK 1 REFERENCE 2
REMARK 1 AUTH Z.SZELTNER,D.REA,T.JUHASZ,V.RENNER,Z.MUCSI,G.OROSZ,V.FULOP,
REMARK 1 AUTH 2 L.POLGAR
REMARK 1 TITL SUBSTRATE-DEPENDENT COMPETENCY OF THE CATALYTIC TRIAD OF
REMARK 1 TITL 2 PROLYL OLIGOPEPTIDASE
REMARK 1 REF J.BIOL.CHEM. V. 277 44597 2002
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 12228249
REMARK 1 DOI 10.1074/JBC.M207386200
REMARK 1 REFERENCE 3
REMARK 1 AUTH V.FULOP,Z.SZELTNER,V.RENNER,L.POLGAR
REMARK 1 TITL STRUCTURES OF PROLYL OLIGOPEPTIDASE SUBSTRATE/ INHIBITOR
REMARK 1 TITL 2 COMPLEXES. USE OF INHIBITOR BINDING FOR TITRATION OF THE
REMARK 1 TITL 3 CATALYTIC HISTIDINE RESIDUE
REMARK 1 REF J.BIOL.CHEM. V. 276 1262 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 11031266
REMARK 1 DOI 10.1074/JBC.M007003200
REMARK 1 REFERENCE 4
REMARK 1 AUTH V.FULOP,Z.SZELTNER,L.POLGAR
REMARK 1 TITL CATALYSIS OF SERINE OLIGOPEPTIDASES IS CONTROLLED BY A
REMARK 1 TITL 2 GATING FILTER MECHANISM
REMARK 1 REF EMBO REP. V. 1 277 2000
REMARK 1 REFN ISSN 1469-221X
REMARK 1 PMID 11256612
REMARK 1 DOI 10.1093/EMBO-REPORTS/KVD048
REMARK 1 REFERENCE 5
REMARK 1 AUTH V.FULOP,Z.BOCSKEI
REMARK 1 TITL PROLYL OLIGOPEPTIDASE: AN UNUSUAL BETA-PROPELLER DOMAIN
REMARK 1 TITL 2 REGULATES PROTEOLYSIS
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 94 161 1998
REMARK 1 REFN ISSN 0092-8674
REMARK 1 PMID 9695945
REMARK 1 DOI 10.1016/S0092-8674(00)81416-6
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 41394
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1827
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5734
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 532
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.72000
REMARK 3 B22 (A**2) : -1.67000
REMARK 3 B33 (A**2) : 0.95000
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): 0.197
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.173
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.663
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UOQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1290013561.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.488
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43221
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 36.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.12900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1H2Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE REFERENCE 5, PH 8.50
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 35.15000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.90000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.90000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.15000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.55000
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 300 REMARK: THE DIMERIC ASSEMBLY DESCRIBED HERE IS DUE
REMARK 300 TO A COMPLEXOF THE PROTEIN CHAIN A WITH A
REMARK 300 PEPTIDE (CHAIN B). CHAIN AIS ESSENTIALLY A MONOMER
REMARK 300 IN THE PHYSIOLOGICAL STATE.
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED MUTATION IN CHAIN A, SER 554 ALA
REMARK 400 THE MUTATED REGION CORREPONDS TO THE ACT_SITE CHARGE RELAY
REMARK 400 OF THE SEQUENCE
REMARK 400
REMARK 400 CLEAVES PEPTIDE BONDS ON THE C-TERMINAL SIDE OF PROLYL
REMARK 400 RESIDUES WITHIN PEPTIDES OF UP TO APPROXIMATELY 30 AMINO
REMARK 400 ACIDS IN LENGTH. BELONGS TO PEPTIDASE FAMILY S9A.
REMARK 400
REMARK 400 CATALYTIC ACTIVITY: HYDROLYSIS OF PRO-|-XAA >> ALA-|-XAA IN
REMARK 400 OLIGOPEPTIDES.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2136 O HOH A 2417 3656 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 18 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 CYS A 57 CA - CB - SG ANGL. DEV. = -11.1 DEGREES
REMARK 500 ASP A 104 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 242 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP A 291 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 LEU A 351 CB - CG - CD2 ANGL. DEV. = 11.7 DEGREES
REMARK 500 ASP A 463 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 642 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 695 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
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 ARG A 306 107.13 -57.01
REMARK 500 SER A 308 80.64 -150.31
REMARK 500 TYR A 311 150.00 74.32
REMARK 500 LYS A 335 -41.00 -138.50
REMARK 500 SER A 346 -63.05 63.65
REMARK 500 GLU A 378 -177.91 -66.40
REMARK 500 TYR A 473 -75.95 -127.18
REMARK 500 LEU A 520 -121.78 59.05
REMARK 500 ALA A 554 -111.07 66.95
REMARK 500 THR A 590 -106.28 23.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 405 ILE A 406 145.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1711
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1712
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E5T RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT
REMARK 900 RELATED ID: 1E8M RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT, COMPLEXED WITH
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 1E8N RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT, COMPLEXED WITH
REMARK 900 PEPTIDE
REMARK 900 RELATED ID: 1H2W RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN
REMARK 900 RELATED ID: 1H2X RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT
REMARK 900 RELATED ID: 1H2Y RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT WITH
REMARK 900 COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL
REMARK 900 RELATED ID: 1H2Z RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND
REMARK 900 PEPTIDE LIGAND SUC- GLY-PRO
REMARK 900 RELATED ID: 1O6F RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND
REMARK 900 PEPTIDE LIGAND SUC- GLY-PRO
REMARK 900 RELATED ID: 1O6G RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641N MUTANT WITH BOUND
REMARK 900 PEPTIDE LIGAND SUC- GLY-PRO
REMARK 900 RELATED ID: 1QFM RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE
REMARK 900 RELATED ID: 1QFS RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE WITH COVALENTLY BOUND
REMARK 900 INHIBITOR Z-PRO-PROLINAL
REMARK 900 RELATED ID: 1UOO RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND
REMARK 900 PEPTIDE LIGAND GLY-PHE-ARG-PRO
REMARK 900 RELATED ID: 1UOP RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND
REMARK 900 PEPTIDE LIGAND GLY-PHE-GLU-PRO
DBREF 1UOQ A 1 710 UNP P23687 PPCE_PIG 1 710
DBREF 1UOQ B 723 726 PDB 1UOQ 1UOQ 723 726
SEQADV 1UOQ ALA A 554 UNP P23687 SER 554 ENGINEERED MUTATION
SEQRES 1 A 710 MET LEU SER PHE GLN TYR PRO ASP VAL TYR ARG ASP GLU
SEQRES 2 A 710 THR ALA ILE GLN ASP TYR HIS GLY HIS LYS VAL CYS ASP
SEQRES 3 A 710 PRO TYR ALA TRP LEU GLU ASP PRO ASP SER GLU GLN THR
SEQRES 4 A 710 LYS ALA PHE VAL GLU ALA GLN ASN LYS ILE THR VAL PRO
SEQRES 5 A 710 PHE LEU GLU GLN CYS PRO ILE ARG GLY LEU TYR LYS GLU
SEQRES 6 A 710 ARG MET THR GLU LEU TYR ASP TYR PRO LYS TYR SER CYS
SEQRES 7 A 710 HIS PHE LYS LYS GLY LYS ARG TYR PHE TYR PHE TYR ASN
SEQRES 8 A 710 THR GLY LEU GLN ASN GLN ARG VAL LEU TYR VAL GLN ASP
SEQRES 9 A 710 SER LEU GLU GLY GLU ALA ARG VAL PHE LEU ASP PRO ASN
SEQRES 10 A 710 ILE LEU SER ASP ASP GLY THR VAL ALA LEU ARG GLY TYR
SEQRES 11 A 710 ALA PHE SER GLU ASP GLY GLU TYR PHE ALA TYR GLY LEU
SEQRES 12 A 710 SER ALA SER GLY SER ASP TRP VAL THR ILE LYS PHE MET
SEQRES 13 A 710 LYS VAL ASP GLY ALA LYS GLU LEU PRO ASP VAL LEU GLU
SEQRES 14 A 710 ARG VAL LYS PHE SER CYS MET ALA TRP THR HIS ASP GLY
SEQRES 15 A 710 LYS GLY MET PHE TYR ASN ALA TYR PRO GLN GLN ASP GLY
SEQRES 16 A 710 LYS SER ASP GLY THR GLU THR SER THR ASN LEU HIS GLN
SEQRES 17 A 710 LYS LEU TYR TYR HIS VAL LEU GLY THR ASP GLN SER GLU
SEQRES 18 A 710 ASP ILE LEU CYS ALA GLU PHE PRO ASP GLU PRO LYS TRP
SEQRES 19 A 710 MET GLY GLY ALA GLU LEU SER ASP ASP GLY ARG TYR VAL
SEQRES 20 A 710 LEU LEU SER ILE ARG GLU GLY CYS ASP PRO VAL ASN ARG
SEQRES 21 A 710 LEU TRP TYR CYS ASP LEU GLN GLN GLU SER ASN GLY ILE
SEQRES 22 A 710 THR GLY ILE LEU LYS TRP VAL LYS LEU ILE ASP ASN PHE
SEQRES 23 A 710 GLU GLY GLU TYR ASP TYR VAL THR ASN GLU GLY THR VAL
SEQRES 24 A 710 PHE THR PHE LYS THR ASN ARG HIS SER PRO ASN TYR ARG
SEQRES 25 A 710 LEU ILE ASN ILE ASP PHE THR ASP PRO GLU GLU SER LYS
SEQRES 26 A 710 TRP LYS VAL LEU VAL PRO GLU HIS GLU LYS ASP VAL LEU
SEQRES 27 A 710 GLU TRP VAL ALA CYS VAL ARG SER ASN PHE LEU VAL LEU
SEQRES 28 A 710 CYS TYR LEU HIS ASP VAL LYS ASN THR LEU GLN LEU HIS
SEQRES 29 A 710 ASP LEU ALA THR GLY ALA LEU LEU LYS ILE PHE PRO LEU
SEQRES 30 A 710 GLU VAL GLY SER VAL VAL GLY TYR SER GLY GLN LYS LYS
SEQRES 31 A 710 ASP THR GLU ILE PHE TYR GLN PHE THR SER PHE LEU SER
SEQRES 32 A 710 PRO GLY ILE ILE TYR HIS CYS ASP LEU THR LYS GLU GLU
SEQRES 33 A 710 LEU GLU PRO ARG VAL PHE ARG GLU VAL THR VAL LYS GLY
SEQRES 34 A 710 ILE ASP ALA SER ASP TYR GLN THR VAL GLN ILE PHE TYR
SEQRES 35 A 710 PRO SER LYS ASP GLY THR LYS ILE PRO MET PHE ILE VAL
SEQRES 36 A 710 HIS LYS LYS GLY ILE LYS LEU ASP GLY SER HIS PRO ALA
SEQRES 37 A 710 PHE LEU TYR GLY TYR GLY GLY PHE ASN ILE SER ILE THR
SEQRES 38 A 710 PRO ASN TYR SER VAL SER ARG LEU ILE PHE VAL ARG HIS
SEQRES 39 A 710 MET GLY GLY VAL LEU ALA VAL ALA ASN ILE ARG GLY GLY
SEQRES 40 A 710 GLY GLU TYR GLY GLU THR TRP HIS LYS GLY GLY ILE LEU
SEQRES 41 A 710 ALA ASN LYS GLN ASN CYS PHE ASP ASP PHE GLN CYS ALA
SEQRES 42 A 710 ALA GLU TYR LEU ILE LYS GLU GLY TYR THR SER PRO LYS
SEQRES 43 A 710 ARG LEU THR ILE ASN GLY GLY ALA ASN GLY GLY LEU LEU
SEQRES 44 A 710 VAL ALA THR CYS ALA ASN GLN ARG PRO ASP LEU PHE GLY
SEQRES 45 A 710 CYS VAL ILE ALA GLN VAL GLY VAL MET ASP MET LEU LYS
SEQRES 46 A 710 PHE HIS LYS TYR THR ILE GLY HIS ALA TRP THR THR ASP
SEQRES 47 A 710 TYR GLY CYS SER ASP SER LYS GLN HIS PHE GLU TRP LEU
SEQRES 48 A 710 ILE LYS TYR SER PRO LEU HIS ASN VAL LYS LEU PRO GLU
SEQRES 49 A 710 ALA ASP ASP ILE GLN TYR PRO SER MET LEU LEU LEU THR
SEQRES 50 A 710 ALA ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER LEU
SEQRES 51 A 710 LYS PHE ILE ALA THR LEU GLN TYR ILE VAL GLY ARG SER
SEQRES 52 A 710 ARG LYS GLN ASN ASN PRO LEU LEU ILE HIS VAL ASP THR
SEQRES 53 A 710 LYS ALA GLY HIS GLY ALA GLY LYS PRO THR ALA LYS VAL
SEQRES 54 A 710 ILE GLU GLU VAL SER ASP MET PHE ALA PHE ILE ALA ARG
SEQRES 55 A 710 CYS LEU ASN ILE ASP TRP ILE PRO
SEQRES 1 B 4 GLU PHE SER PRO
HET GOL A1711 6
HET GOL A1712 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *532(H2 O)
HELIX 1 1 TYR A 28 ASP A 33 5 6
HELIX 2 2 SER A 36 GLN A 56 1 21
HELIX 3 3 PRO A 58 ASP A 72 1 15
HELIX 4 4 ASP A 115 SER A 120 5 6
HELIX 5 5 ASP A 218 ASP A 222 5 5
HELIX 6 6 GLN A 267 GLU A 269 5 3
HELIX 7 7 GLU A 322 TRP A 326 5 5
HELIX 8 8 ASP A 431 SER A 433 5 3
HELIX 9 9 SER A 485 GLY A 496 1 12
HELIX 10 10 TYR A 510 GLY A 517 1 8
HELIX 11 11 GLY A 518 ALA A 521 5 4
HELIX 12 12 ASN A 522 GLU A 540 1 19
HELIX 13 13 SER A 544 LYS A 546 5 3
HELIX 14 14 ALA A 554 ARG A 567 1 14
HELIX 15 15 PRO A 568 PHE A 571 5 4
HELIX 16 16 LYS A 585 TYR A 589 5 5
HELIX 17 17 ILE A 591 ALA A 594 5 4
HELIX 18 18 TRP A 595 GLY A 600 1 6
HELIX 19 19 SER A 604 SER A 615 1 12
HELIX 20 20 PRO A 616 ASN A 619 5 4
HELIX 21 21 PRO A 646 VAL A 660 1 15
HELIX 22 22 PRO A 685 ASN A 705 1 21
SHEET 1 AA 2 ILE A 16 TYR A 19 0
SHEET 2 AA 2 HIS A 22 CYS A 25 -1 O HIS A 22 N TYR A 19
SHEET 1 AB 3 LYS A 75 TYR A 76 0
SHEET 2 AB 3 ARG A 85 ASN A 91 -1 O ASN A 91 N LYS A 75
SHEET 3 AB 3 PHE A 80 LYS A 82 -1 O PHE A 80 N PHE A 87
SHEET 1 AC 4 LYS A 75 TYR A 76 0
SHEET 2 AC 4 ARG A 85 ASN A 91 -1 O ASN A 91 N LYS A 75
SHEET 3 AC 4 VAL A 99 GLN A 103 -1 O VAL A 99 N TYR A 90
SHEET 4 AC 4 ARG A 111 LEU A 114 -1 O ARG A 111 N VAL A 102
SHEET 1 AD 4 VAL A 125 PHE A 132 0
SHEET 2 AD 4 TYR A 138 ALA A 145 -1 O ALA A 140 N ALA A 131
SHEET 3 AD 4 VAL A 151 LYS A 157 -1 O THR A 152 N LEU A 143
SHEET 4 AD 4 LYS A 162 VAL A 171 -1 O LYS A 162 N LYS A 157
SHEET 1 AE 4 ALA A 177 TRP A 178 0
SHEET 2 AE 4 GLY A 184 ALA A 189 -1 O PHE A 186 N ALA A 177
SHEET 3 AE 4 LYS A 209 VAL A 214 -1 O LYS A 209 N ALA A 189
SHEET 4 AE 4 ILE A 223 ALA A 226 -1 O ILE A 223 N TYR A 212
SHEET 1 AF 4 MET A 235 LEU A 240 0
SHEET 2 AF 4 TYR A 246 ARG A 252 -1 O LEU A 248 N GLU A 239
SHEET 3 AF 4 ARG A 260 ASP A 265 -1 O ARG A 260 N ILE A 251
SHEET 4 AF 4 VAL A 280 ILE A 283 -1 O VAL A 280 N TYR A 263
SHEET 1 AG 4 TYR A 290 GLU A 296 0
SHEET 2 AG 4 VAL A 299 THR A 304 -1 O VAL A 299 N GLU A 296
SHEET 3 AG 4 ARG A 312 ASP A 317 -1 O ARG A 312 N THR A 304
SHEET 4 AG 4 LYS A 327 VAL A 330 -1 O LYS A 327 N ASN A 315
SHEET 1 AH 4 VAL A 337 VAL A 344 0
SHEET 2 AH 4 PHE A 348 HIS A 355 -1 O PHE A 348 N VAL A 344
SHEET 3 AH 4 LYS A 358 ASP A 365 -1 O LYS A 358 N HIS A 355
SHEET 4 AH 4 LEU A 371 PHE A 375 -1 N LEU A 372 O LEU A 363
SHEET 1 AI 4 SER A 381 SER A 386 0
SHEET 2 AI 4 GLU A 393 THR A 399 -1 O PHE A 395 N SER A 386
SHEET 3 AI 4 ILE A 406 ASP A 411 -1 O ILE A 406 N PHE A 398
SHEET 4 AI 4 ARG A 420 GLU A 424 -1 O ARG A 420 N HIS A 409
SHEET 1 AJ 8 TYR A 435 PRO A 443 0
SHEET 2 AJ 8 LYS A 449 LYS A 457 -1 O ILE A 450 N TYR A 442
SHEET 3 AJ 8 VAL A 498 ALA A 502 -1 O LEU A 499 N VAL A 455
SHEET 4 AJ 8 ALA A 468 TYR A 471 1 O PHE A 469 N ALA A 500
SHEET 5 AJ 8 LEU A 548 GLY A 553 1 O THR A 549 N LEU A 470
SHEET 6 AJ 8 CYS A 573 GLN A 577 1 O CYS A 573 N ILE A 550
SHEET 7 AJ 8 SER A 632 ALA A 638 1 O SER A 632 N VAL A 574
SHEET 8 AJ 8 LEU A 670 ASP A 675 1 O LEU A 671 N LEU A 635
SITE 1 AC1 7 ILE A 118 LEU A 119 SER A 120 ASP A 121
SITE 2 AC1 7 ASP A 446 ASN A 522 ASN A 525
SITE 1 AC2 7 ALA A 226 GLU A 227 PHE A 228 TRP A 262
SITE 2 AC2 7 ILE A 276 LYS A 281 HOH A2530
CRYST1 70.300 99.100 109.800 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 0.014225 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010091 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009107 0.00000
(ATOM LINES ARE NOT SHOWN.)
END