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HEADER HYDROLASE 20-AUG-02 1H2X
TITLE PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 SYNONYM: POST-PROLINE CLEAVING ENZYME, PE;
COMPND 4 EC: 3.4.21.26;
COMPND 5 CHAIN: A;
COMPND 6 MUTATION: YES;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: ENGINEERED MUTATION TYR 473 PHE
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 4 ORGANISM_COMMON: PIG;
SOURCE 5 TISSUE: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS HYDROLASE, PROLYL OLIGOPEPTIDASE, AMNESIA, ALPHA/
KEYWDS 2 BETA-HYDROLASE, BETA-PROPELLER, SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.FULOP
REVDAT 1 11-NOV-02 1H2X 0
JRNL AUTH Z.SZELTNER,D.REA,V.RENNER,V.FULOP,L.POLGAR
JRNL TITL ELECTROSTATIC EFFECTS AND BINDING DETERMINANTS IN
JRNL TITL 2 THE CATALYSIS OF PROLYL OLIGOPEPTIDASE: SITE
JRNL TITL 3 SPECIFIC MUTAGENESIS AT THE OXYANION BINDING SITE
JRNL REF J.BIOL.CHEM. V. 277 42613 2002
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.FULOP,Z.SZELTNER,V.RENNER,L.POLGAR
REMARK 1 TITL STRUCTURES OF PROLYL OLIGOPEPTIDASE SUBSTRATE/
REMARK 1 TITL 2 INHIBITOR COMPLEXES. USE OF INHIBITOR BINDING FOR
REMARK 1 TITL 3 TITRATION OF THE CATALYTIC HISTIDINE RESIDUE
REMARK 1 REF J.BIOL.CHEM. V. 276 1262 2001
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH V.FULOP,Z.SZELTNER,L.POLGAR
REMARK 1 TITL CATALYSIS OF SERINE OLIGOPEPTIDASES IS CONTROLLED
REMARK 1 TITL 2 BY A GATING FILTER MECHANISM
REMARK 1 REF EMBO REPORTS V. 1 277 2000
REMARK 1 REFN ASTM UK ISSN 1469-3178
REMARK 1 REFERENCE 3
REMARK 1 AUTH V.FULOP,Z.BOCSKEI,L.POLGAR
REMARK 1 TITL PROLYL OLIGOPEPTIDASE: AN UNUSUAL BETA-PROPELLER
REMARK 1 TITL 2 DOMAIN REGULATES PROTEOLYSIS
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 94 161 1998
REMARK 1 REFN ASTM CELLB5 US ISSN 0092-8674
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 127909
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 SET) : 0.175
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.0
REMARK 3 FREE R VALUE TEST SET COUNT : 5215
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5700
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 1065
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : 0.09
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.4
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1H2X COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 20-AUG-2002.
REMARK 100 THE EBI ID CODE IS EBI-11274.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX-LAB BEAMLINE 711
REMARK 200 BEAMLINE : BL-711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.021
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128812
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.49
REMARK 200 RESOLUTION RANGE LOW (A) : 26.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.2
REMARK 200 R MERGE (I) : 0.036
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 37.2
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.2
REMARK 200 R MERGE FOR SHELL (I) : 0.097
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 9.6
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4, X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1QFM
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE REFERENCE 3
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 35.60000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.55000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.55000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.60000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.90000
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 400
REMARK 400 COMPOUND
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 CHAIN A ENGINEERED MUTATION TYR 473 PHE
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN A 91 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 VAL A 125 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 THR A 152 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 LYS A 157 N - CA - C ANGL. DEV. = -11.1 DEGREES
REMARK 500 SER A 174 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 VAL A 247 N - CA - C ANGL. DEV. = -10.0 DEGREES
REMARK 500 ARG A 260 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 VAL A 280 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 GLU A 296 N - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500 LYS A 303 N - CA - C ANGL. DEV. = -10.7 DEGREES
REMARK 500 ASP A 320 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 PRO A 321 N - CA - C ANGL. DEV. = 12.8 DEGREES
REMARK 500 LEU A 338 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 LEU A 351 CA - CB - CG ANGL. DEV. = 11.9 DEGREES
REMARK 500 THR A 360 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 VAL A 382 N - CA - C ANGL. DEV. = -10.3 DEGREES
REMARK 500 PRO A 467 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 GLY A 600 N - CA - C ANGL. DEV. = -8.9 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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 TYR A 311 151.81 73.03
REMARK 500 SER A 346 -60.39 68.24
REMARK 500 SER A 554 -117.67 64.81
REMARK 500 THR A 590 -111.57 31.61
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
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: AS1
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE: CATALYTIC TRIAD
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E5T RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN,
REMARK 900 MUTANT
REMARK 900 RELATED ID: 1E8M RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN,
REMARK 900 MUTANT, COMPLEXED WITH INHIBITOR
REMARK 900 RELATED ID: 1E8N RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN,
REMARK 900 MUTANT, COMPLEXED WITH PEPTIDE
REMARK 900 RELATED ID: 1H2W RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN
REMARK 900 RELATED ID: 1H2Y RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN,
REMARK 900 Y473F MUTANT WITH COVALENTLY BOUND INHIBITOR
REMARK 900 Z-PRO-PROLINAL
REMARK 900 RELATED ID: 1H2Z RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN,
REMARK 900 S554A MUTANT BOUND PEPTIDE LIGAND SUC-GLY-PRO
REMARK 900 RELATED ID: 1O6F RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN,
REMARK 900 D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-
REMARK 900 GLY-PRO
REMARK 900 RELATED ID: 1O6G RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN,
REMARK 900 D641N MUTANT WITH BOUND PEPTIDE LIGAND SUC-
REMARK 900 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
REMARK 900 COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL
DBREF 1H2X A 1 710 SWS P23687 PPCE_PIG 1 710
SEQADV 1H2X PHE A 473 SWS P23687 TYR 473 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 PHE 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 SER 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
HET GOL A 791 6
HET GOL A 792 6
HET GOL A 793 6
HET GOL A 794 6
HETNAM GOL GLYCEROL
FORMUL 2 GOL 4(C3 H8 O3)
FORMUL 3 HOH *1065(H2 O1)
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 TYR A 71 1 14
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 ASN A 522 5 5
HELIX 12 12 LYS A 523 GLU A 540 1 18
HELIX 13 13 SER A 544 LYS A 546 5 3
HELIX 14 14 SER 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 MET A 176 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 PRO A 419 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 AS1 3 SER A 554 ASP A 641 HIS A 680
SITE 1 AC1 8 ALA A 226 GLU A 227 PHE A 228 TRP A 262
SITE 2 AC1 8 ILE A 276 LYS A 281 HOH Z1058 HOH Z1059
SITE 1 AC2 11 PRO A 568 ASP A 569 PHE A 571 GLY A 572
SITE 2 AC2 11 ILE A 628 GLN A 629 PRO A 631 ASN A 668
SITE 3 AC2 11 HOH Z 972 HOH Z1060 HOH Z1061
SITE 1 AC3 5 ALA A 342 TYR A 385 HOH Z 723 HOH Z1062
SITE 2 AC3 5 HOH Z1063
SITE 1 AC4 7 PHE A 173 MET A 235 SER A 250 ARG A 252
SITE 2 AC4 7 HOH Z 394 HOH Z 471 HOH Z1065
CRYST1 71.200 99.800 111.100 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 0.014045 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010020 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009001 0.00000
TER 5701 PRO A 710
MASTER 339 0 4 22 41 0 10 6 6789 1 24 55
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