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HEADER HYDROLASE 08-JUN-12 4AX4
TITLE PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, H680A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL OLIGOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PE, POST-PROLINE CLEAVING ENZYME;
COMPND 5 EC: 3.4.21.26;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, AMNESIA, ALPHA/BETA-HYDROLASE, BETA-PROPELLER, SERINE
KEYWDS 2 PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.SZELTNER,T.JUHASZ,I.SZAMOSI,D.REA,V.FULOP,K.MODOS,L.JULIANO,
AUTHOR 2 L.POLGAR
REVDAT 1 26-SEP-12 4AX4 0
JRNL AUTH Z.SZELTNER,T.JUHASZ,I.SZAMOSI,D.REA,V.FULOP,K.MODOS,
JRNL AUTH 2 L.JULIANO,L.POLGAR
JRNL TITL THE LOOPS FACING THE ACTIVE SITE OF PROLYL OLIGOPEPTIDASE
JRNL TITL 2 ARE CRUCIAL COMPONENTS IN SUBSTRATE GATING AND SPECIFICITY.
JRNL REF BIOCHIM.BIOPHYS.ACTA 2012
JRNL REFN ESSN 0006-3002
JRNL PMID 22940581
JRNL DOI 10.1016/J.BBAPAP.2012.08.012
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.15
REMARK 3 NUMBER OF REFLECTIONS : 96969
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) : 0.16368
REMARK 3 R VALUE (WORKING SET) : 0.16229
REMARK 3 FREE R VALUE : 0.19577
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.1
REMARK 3 FREE R VALUE TEST SET COUNT : 4116
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) : 1.600
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.642
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7118
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.303
REMARK 3 BIN FREE R VALUE SET COUNT : 315
REMARK 3 BIN FREE R VALUE : 0.318
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5623
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 767
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.3
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.317
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08
REMARK 3 B22 (A**2) : -0.24
REMARK 3 B33 (A**2) : 0.16
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): 0.080
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.258
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5820 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7878 ; 1.509 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 698 ; 6.100 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 279 ;34.506 ;24.229
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 957 ;12.151 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;19.416 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 832 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4449 ; 0.009 ; 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): 3475 ; 0.944 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5611 ; 1.723 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2345 ; 2.811 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2267 ; 4.475 ; 4.500
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 : 3
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 1 A 72
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2950 49.1160 65.2050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0507 T22: 0.0142
REMARK 3 T33: 0.0452 T12: -0.0027
REMARK 3 T13: 0.0160 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 0.6847 L22: 0.0920
REMARK 3 L33: 0.9345 L12: -0.1217
REMARK 3 L13: -0.5532 L23: 0.1360
REMARK 3 S TENSOR
REMARK 3 S11: -0.0534 S12: 0.0460 S13: 0.0171
REMARK 3 S21: -0.0354 S22: 0.0000 S23: -0.0235
REMARK 3 S31: -0.0186 S32: -0.0046 S33: 0.0533
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 73 A 427
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6540 40.3020 101.6090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0175 T22: 0.0181
REMARK 3 T33: 0.0010 T12: 0.0032
REMARK 3 T13: -0.0032 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.3232 L22: 0.3936
REMARK 3 L33: 0.2127 L12: -0.0245
REMARK 3 L13: 0.0335 L23: -0.0169
REMARK 3 S TENSOR
REMARK 3 S11: -0.0138 S12: -0.0208 S13: -0.0004
REMARK 3 S21: 0.0044 S22: 0.0150 S23: -0.0101
REMARK 3 S31: -0.0241 S32: 0.0058 S33: -0.0012
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 428 A 710
REMARK 3 ORIGIN FOR THE GROUP (A): 25.2550 38.8860 75.9510
REMARK 3 T TENSOR
REMARK 3 T11: 0.0164 T22: 0.0155
REMARK 3 T33: 0.0202 T12: 0.0046
REMARK 3 T13: -0.0016 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.2864 L22: 0.4648
REMARK 3 L33: 0.6661 L12: 0.0463
REMARK 3 L13: -0.1607 L23: -0.2953
REMARK 3 S TENSOR
REMARK 3 S11: -0.0352 S12: 0.0020 S13: -0.0146
REMARK 3 S21: -0.0722 S22: -0.0153 S23: 0.0006
REMARK 3 S31: 0.0542 S32: -0.0459 S33: 0.0505
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. RESIDUES 192-201 ARE DISORDERED AND NOT
REMARK 3 MODELLED.
REMARK 4
REMARK 4 4AX4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-12.
REMARK 100 THE PDBE ID CODE IS EBI-52822.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
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 : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315R)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101085
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.8
REMARK 200 R MERGE FOR SHELL (I) : 0.78
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
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 1QFM
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% METHOXY-POLYETHYLENE
REMARK 280 GLYCOL (MPEG) 5K, 20 MM CA(OAC)2, 0.1 M TRIS PH 8.5, 15%
REMARK 280 GLYCEROL
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 35.54000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.03000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.54000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.03000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.54000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.54000
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
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 RESIDUE IN CHAIN A, HIS 680 TO ALA
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 GLN A 192
REMARK 465 GLN A 193
REMARK 465 ASP A 194
REMARK 465 GLY A 195
REMARK 465 LYS A 196
REMARK 465 SER A 197
REMARK 465 ASP A 198
REMARK 465 GLY A 199
REMARK 465 THR A 200
REMARK 465 GLU A 201
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 OD2 ASP A 218 O HOH A 2343 2.13
REMARK 500 OE2 GLU A 221 O HOH A 2342 1.98
REMARK 500 O HOH A 2175 O HOH A 2431 2.07
REMARK 500 O HOH A 2498 O HOH A 2521 2.11
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 CYS A 526 CB - CA - C ANGL. DEV. = -8.1 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 SER A 3 42.34 -94.80
REMARK 500 SER A 308 77.63 -154.12
REMARK 500 TYR A 311 152.48 78.56
REMARK 500 LYS A 335 -41.32 -132.39
REMARK 500 SER A 346 -59.21 71.46
REMARK 500 TYR A 473 -78.12 -130.41
REMARK 500 LEU A 520 -126.00 56.95
REMARK 500 SER A 554 -116.88 68.73
REMARK 500 THR A 590 -120.42 41.07
REMARK 500 ALA A 678 119.38 -26.94
REMARK 500 ALA A 680 -169.71 -100.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1711
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1712
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1713
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1714
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1715
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1716
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1717
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1718
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1719
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,
REMARK 900 COMPLEXED WITH INHIBITOR
REMARK 900 RELATED ID: 1E8N RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT,
REMARK 900 COMPLEXED WITH 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
REMARK 900 WITH COVALENTLY BOUND INHIBITOR Z-PRO-PROLINAL
REMARK 900 RELATED ID: 1H2Z RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT
REMARK 900 WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO
REMARK 900 RELATED ID: 1O6F RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT
REMARK 900 WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO
REMARK 900 RELATED ID: 1O6G RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641N MUTANT
REMARK 900 WITH BOUND 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
REMARK 900 BOUND INHIBITOR Z-PRO-PROLINAL
REMARK 900 RELATED ID: 1UOO RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT
REMARK 900 WITH BOUND PEPTIDE LIGAND GLY-PHE-ARG-PRO
REMARK 900 RELATED ID: 1UOP RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT
REMARK 900 WITH BOUND PEPTIDE LIGAND GLY-PHE-GLU-PRO
REMARK 900 RELATED ID: 1UOQ RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT
REMARK 900 WITH BOUND PEPTIDE LIGAND GLU-PHE-SER-PRO
REMARK 900 RELATED ID: 1VZ2 RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/
REMARK 900 C255T MUTANT
REMARK 900 RELATED ID: 1VZ3 RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, T597C MUTANT
REMARK 900 RELATED ID: 2XDW RELATED DB: PDB
REMARK 900 INHIBITION OF PROLYL OLIGOPEPTIDASE WITH A SYNTHETIC
REMARK 900 UNNATURAL DIPEPTIDE
REMARK 900 RELATED ID: 4AMY RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A
REMARK 900 COVALENTLY BOUND INHIBITOR IC-1
REMARK 900 RELATED ID: 4AMZ RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A
REMARK 900 COVALENTLY BOUND INHIBITOR IC-2
REMARK 900 RELATED ID: 4AN0 RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A
REMARK 900 COVALENTLY BOUND INHIBITOR IC-3
REMARK 900 RELATED ID: 4AN1 RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A
REMARK 900 COVALENTLY BOUND INHIBITOR IC-4
DBREF 4AX4 A 1 710 UNP P23687 PPCE_PIG 1 710
SEQADV 4AX4 ALA A 680 UNP P23687 HIS 680 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 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 ALA 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 A1711 6
HET GOL A1712 6
HET GOL A1713 6
HET GOL A1714 6
HET GOL A1715 6
HET GOL A1716 6
HET GOL A1717 6
HET GOL A1718 6
HET GOL A1719 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 9(C3 H8 O3)
FORMUL 3 HOH *767(H2 O)
HELIX 1 1 TYR A 28 ASP A 33 5 6
HELIX 2 2 SER A 36 CYS A 57 1 22
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 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 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 2 LYS A 75 TYR A 76 0
SHEET 2 AB 2 ARG A 85 ASN A 91 -1 O ASN A 91 N LYS A 75
SHEET 1 AC 2 PHE A 80 LYS A 82 0
SHEET 2 AC 2 ARG A 85 ASN A 91 -1 O ARG A 85 N LYS A 82
SHEET 1 AD 4 ALA A 110 LEU A 114 0
SHEET 2 AD 4 VAL A 99 GLN A 103 -1 O LEU A 100 N PHE A 113
SHEET 3 AD 4 ARG A 85 ASN A 91 -1 O TYR A 86 N GLN A 103
SHEET 4 AD 4 PHE A 80 LYS A 82 -1 O PHE A 80 N PHE A 87
SHEET 1 AE 4 ALA A 110 LEU A 114 0
SHEET 2 AE 4 VAL A 99 GLN A 103 -1 O LEU A 100 N PHE A 113
SHEET 3 AE 4 ARG A 85 ASN A 91 -1 O TYR A 86 N GLN A 103
SHEET 4 AE 4 LYS A 75 TYR A 76 -1 O LYS A 75 N ASN A 91
SHEET 1 AF 7 VAL A 125 PHE A 132 0
SHEET 2 AF 7 TYR A 138 ALA A 145 -1 O ALA A 140 N ALA A 131
SHEET 3 AF 7 TRP A 150 LYS A 157 -1 O THR A 152 N LEU A 143
SHEET 4 AF 7 LYS A 162 TRP A 178 -1 O LYS A 162 N LYS A 157
SHEET 5 AF 7 GLY A 184 ALA A 189 -1 O PHE A 186 N ALA A 177
SHEET 6 AF 7 LYS A 209 VAL A 214 -1 O LYS A 209 N ALA A 189
SHEET 7 AF 7 ILE A 223 ALA A 226 -1 O ILE A 223 N TYR A 212
SHEET 1 AG 4 MET A 235 LEU A 240 0
SHEET 2 AG 4 TYR A 246 ARG A 252 -1 O LEU A 248 N GLU A 239
SHEET 3 AG 4 ARG A 260 ASP A 265 -1 O ARG A 260 N ILE A 251
SHEET 4 AG 4 VAL A 280 ILE A 283 -1 O VAL A 280 N TYR A 263
SHEET 1 AH 4 TYR A 290 GLU A 296 0
SHEET 2 AH 4 VAL A 299 THR A 304 -1 O VAL A 299 N GLU A 296
SHEET 3 AH 4 ARG A 312 ASP A 317 -1 O ARG A 312 N THR A 304
SHEET 4 AH 4 LYS A 327 VAL A 330 -1 O LYS A 327 N ASN A 315
SHEET 1 AI 4 VAL A 337 VAL A 344 0
SHEET 2 AI 4 PHE A 348 HIS A 355 -1 O PHE A 348 N VAL A 344
SHEET 3 AI 4 LYS A 358 ASP A 365 -1 O LYS A 358 N HIS A 355
SHEET 4 AI 4 LEU A 371 PHE A 375 -1 N LEU A 372 O LEU A 363
SHEET 1 AJ 4 SER A 381 SER A 386 0
SHEET 2 AJ 4 GLU A 393 SER A 400 -1 O PHE A 395 N SER A 386
SHEET 3 AJ 4 SER A 403 ASP A 411 -1 O SER A 403 N SER A 400
SHEET 4 AJ 4 ARG A 420 VAL A 425 -1 O ARG A 420 N HIS A 409
SHEET 1 AK 8 TYR A 435 PRO A 443 0
SHEET 2 AK 8 LYS A 449 LYS A 457 -1 O ILE A 450 N TYR A 442
SHEET 3 AK 8 VAL A 498 ALA A 502 -1 O LEU A 499 N VAL A 455
SHEET 4 AK 8 ALA A 468 TYR A 471 1 O PHE A 469 N ALA A 500
SHEET 5 AK 8 LEU A 548 GLY A 553 1 O THR A 549 N LEU A 470
SHEET 6 AK 8 CYS A 573 GLN A 577 1 O CYS A 573 N ILE A 550
SHEET 7 AK 8 SER A 632 ALA A 638 1 O SER A 632 N VAL A 574
SHEET 8 AK 8 LEU A 670 ASP A 675 1 O LEU A 671 N LEU A 635
SITE 1 AC1 7 ALA A 226 GLU A 227 PHE A 228 ILE A 276
SITE 2 AC1 7 LYS A 281 HOH A2765 HOH A2766
SITE 1 AC2 9 PRO A 568 ASP A 569 PHE A 571 ILE A 628
SITE 2 AC2 9 GLN A 629 PRO A 631 ASN A 668 HOH A2667
SITE 3 AC2 9 HOH A2740
SITE 1 AC3 8 GLU A 239 ASP A 291 TYR A 292 HOH A2370
SITE 2 AC3 8 HOH A2372 HOH A2441 HOH A2442 HOH A2444
SITE 1 AC4 3 VAL A 341 HOH A2503 HOH A2545
SITE 1 AC5 6 ASP A 8 GLN A 38 PHE A 42 LYS A 183
SITE 2 AC5 6 HOH A2022 HOH A2767
SITE 1 AC6 6 LYS A 546 GLY A 572 SER A 632 ASN A 668
SITE 2 AC6 6 CYS A 703 HOH A2740
SITE 1 AC7 7 ARG A 85 ASP A 104 ARG A 111 VAL A 158
SITE 2 AC7 7 GLY A 160 HOH A2159 HOH A2198
SITE 1 AC8 4 ARG A 170 TYR A 190 TYR A 211 GLN A 219
SITE 1 AC9 4 ARG A 11 CYS A 25 PRO A 27 HOH A2732
CRYST1 71.080 99.080 110.060 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 0.014069 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010093 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009086 0.00000
TER 5624 PRO A 710
MASTER 463 0 9 22 45 0 16 6 6444 1 54 55
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