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HEADER HYDROLASE 07-JUN-07 2Z3W
TITLE PROLYL TRIPEPTIDYL AMINOPEPTIDASE MUTANT E636A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE IV;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 39-732;
COMPND 5 SYNONYM: PROLYL TRIPEPTIDYL AMINOPEPTIDASE;
COMPND 6 EC: 3.4.14.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PORPHYROMONAS GINGIVALIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: W83;
SOURCE 5 GENE: PG1361;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS PROLYL OLIGOPEPTIDASE FAMILY, PEPTIDASE FAMILY S9, SERINE
KEYWDS 2 PROTEASE, PROLINE-SPECIFIC PEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XU,Y.NAKAJIMA,K.ITO,T.YOSHIMOTO
REVDAT 1 19-FEB-08 2Z3W 0
JRNL AUTH Y.XU,Y.NAKAJIMA,K.ITO,H.ZHENG,H.OYAMA,U.HEISER,
JRNL AUTH 2 T.HOFFMANN,U.T.GARTNER,H.U.DEMUTH,T.YOSHIMOTO
JRNL TITL NOVEL INHIBITOR FOR PROLYL TRIPEPTIDYL
JRNL TITL 2 AMINOPEPTIDASE FROM PORPHYROMONAS GINGIVALIS AND
JRNL TITL 3 DETAILS OF SUBSTRATE-RECOGNITION MECHANISM
JRNL REF J.MOL.BIOL. V. 375 708 2008
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 66242
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3533
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4827
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 263
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 5751
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.59000
REMARK 3 B22 (A**2) : -0.59000
REMARK 3 B33 (A**2) : 0.88000
REMARK 3 B12 (A**2) : -0.29000
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): 0.139
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.131
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.074
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5345 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7262 ; 1.449 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 650 ; 6.442 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 251 ;33.639 ;23.147
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 836 ;14.575 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;16.622 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 777 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4134 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2383 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3594 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 554 ; 0.140 ; 0.200
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): 51 ; 0.156 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.159 ; 0.200
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): 3333 ; 0.989 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5228 ; 1.561 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2332 ; 2.402 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2034 ; 3.628 ; 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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 2Z3W COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB027488.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMETER
REMARK 200 OPTICS : MONOCHROMETOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71953
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 20.000
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 81.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 19.10
REMARK 200 R MERGE FOR SHELL (I) : 0.31400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 11.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2D5L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1M POTASSIUM SODIUM TARTRATE,
REMARK 280 0.2M LITHIUM SULFATE, 0.1M CHES BUFFER, PH 9.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X-Y,X,1/2+Z
REMARK 290 3555 -Y,X-Y,Z
REMARK 290 4555 -X,-Y,1/2+Z
REMARK 290 5555 -X+Y,-X,Z
REMARK 290 6555 Y,-X+Y,1/2+Z
REMARK 290 7555 X-Y,-Y,-Z
REMARK 290 8555 -Y,-X,1/2-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -X+Y,Y,1/2-Z
REMARK 290 11555 Y,X,-Z
REMARK 290 12555 X,X-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 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.47150
REMARK 290 SMTRY1 3 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 80.47150
REMARK 290 SMTRY1 5 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 80.47150
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 80.47150
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 80.47150
REMARK 290 SMTRY1 11 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 11 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 80.47150
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: DIMER
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 160.94300
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MET A 27
REMARK 465 ARG A 28
REMARK 465 GLY A 29
REMARK 465 SER A 30
REMARK 465 HIS A 31
REMARK 465 HIS A 32
REMARK 465 HIS A 33
REMARK 465 HIS A 34
REMARK 465 HIS A 35
REMARK 465 HIS A 36
REMARK 465 GLY A 37
REMARK 465 SER A 38
REMARK 465 LEU A 39
REMARK 465 MET A 40
REMARK 465 PRO A 41
REMARK 465 GLY A 42
REMARK 465 GLY A 43
REMARK 465 LYS A 44
REMARK 465 GLU A 45
REMARK 465 PHE A 46
REMARK 465 TYR A 47
REMARK 465 ASN A 48
REMARK 465 PHE A 49
REMARK 465 TYR A 50
REMARK 465 PRO A 51
REMARK 465 GLU A 52
REMARK 465 ALA A 77
REMARK 465 ASN A 78
REMARK 465 GLY A 79
REMARK 465 LYS A 80
REMARK 465 SER A 81
REMARK 465 ALA A 82
REMARK 465 GLN A 83
REMARK 465 GLY A 99
REMARK 465 CYS A 100
REMARK 465 LYS A 101
REMARK 465 PHE A 102
REMARK 465 GLN A 103
REMARK 465 THR A 104
REMARK 465 THR A 105
REMARK 465 ASP A 106
REMARK 465 ALA A 107
REMARK 465 ASN A 471
REMARK 465 PRO A 472
REMARK 465 ASP A 473
REMARK 465 THR A 474
REMARK 465 GLY A 475
REMARK 465 TYR A 476
REMARK 465 SER A 532
REMARK 465 SER A 533
REMARK 465 VAL A 534
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 TYR A 53 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 76 CG CD CE NZ
REMARK 470 GLU A 98 CG CD OE1 OE2
REMARK 470 GLN A 126 CG CD OE1 NE2
REMARK 470 LYS A 470 CG CD CE NZ
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
REMARK 500 O HOH A 922 O HOH A 1035 2.16
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 NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 371 NE - CZ - NH2 ANGL. DEV. = -3.6 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 THR A 140 -70.84 -93.42
REMARK 500 HIS A 167 -13.30 84.86
REMARK 500 LEU A 177 115.64 -34.48
REMARK 500 SER A 404 142.01 179.64
REMARK 500 ARG A 452 126.66 -170.66
REMARK 500 ILE A 459 95.90 -51.86
REMARK 500 TYR A 518 -78.04 -121.02
REMARK 500 HIS A 522 -12.05 76.49
REMARK 500 ARG A 570 41.30 -142.78
REMARK 500 SER A 603 -119.57 72.67
REMARK 500 ASP A 645 -178.04 61.50
REMARK 500 ASN A 650 54.97 -143.48
REMARK 500 GLU A 709 -134.67 -88.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 902
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2D5L RELATED DB: PDB
REMARK 900 THE WILD-TYPE PROTEIN
REMARK 900 RELATED ID: 2DCM RELATED DB: PDB
REMARK 900 THE S603A MUTANT PROTEIN COMPLEXED WITH SUBSTRATE
REMARK 900 RELATED ID: 2EEP RELATED DB: PDB
REMARK 900 THE WILD-TYPE PROTEIN COMPLEXD WITH INHIBITOR
REMARK 900 RELATED ID: 2Z3Z RELATED DB: PDB
REMARK 900 THE SAME MUTANT ENZYME COMPLEXD WITH AN INHIBITOR
DBREF 2Z3W A 39 732 UNP Q7MUW6 Q7MUW6_PORGI 39 732
SEQADV 2Z3W MET A 27 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W ARG A 28 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W GLY A 29 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W SER A 30 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W HIS A 31 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W HIS A 32 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W HIS A 33 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W HIS A 34 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W HIS A 35 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W HIS A 36 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W GLY A 37 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W SER A 38 UNP Q7MUW6 EXPRESSION TAG
SEQADV 2Z3W ALA A 636 UNP Q7MUW6 GLU 636 ENGINEERED
SEQRES 1 A 706 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER LEU
SEQRES 2 A 706 MET PRO GLY GLY LYS GLU PHE TYR ASN PHE TYR PRO GLU
SEQRES 3 A 706 TYR VAL VAL GLY LEU GLN TRP MET GLY ASP ASN TYR VAL
SEQRES 4 A 706 PHE ILE GLU GLY ASP ASP LEU VAL PHE ASN LYS ALA ASN
SEQRES 5 A 706 GLY LYS SER ALA GLN THR THR ARG PHE SER ALA ALA ASP
SEQRES 6 A 706 LEU ASN ALA LEU MET PRO GLU GLY CYS LYS PHE GLN THR
SEQRES 7 A 706 THR ASP ALA PHE PRO SER PHE ARG THR LEU ASP ALA GLY
SEQRES 8 A 706 ARG GLY LEU VAL VAL LEU PHE THR GLN GLY GLY LEU VAL
SEQRES 9 A 706 GLY PHE ASP MET LEU ALA ARG LYS VAL THR TYR LEU PHE
SEQRES 10 A 706 ASP THR ASN GLU GLU THR ALA SER LEU ASP PHE SER PRO
SEQRES 11 A 706 VAL GLY ASP ARG VAL ALA TYR VAL ARG ASN HIS ASN LEU
SEQRES 12 A 706 TYR ILE ALA ARG GLY GLY LYS LEU GLY GLU GLY MET SER
SEQRES 13 A 706 ARG ALA ILE ALA VAL THR ILE ASP GLY THR GLU THR LEU
SEQRES 14 A 706 VAL TYR GLY GLN ALA VAL HIS GLN ARG GLU PHE GLY ILE
SEQRES 15 A 706 GLU LYS GLY THR PHE TRP SER PRO LYS GLY SER CYS LEU
SEQRES 16 A 706 ALA PHE TYR ARG MET ASP GLN SER MET VAL LYS PRO THR
SEQRES 17 A 706 PRO ILE VAL ASP TYR HIS PRO LEU GLU ALA GLU SER LYS
SEQRES 18 A 706 PRO LEU TYR TYR PRO MET ALA GLY THR PRO SER HIS HIS
SEQRES 19 A 706 VAL THR VAL GLY ILE TYR HIS LEU ALA THR GLY LYS THR
SEQRES 20 A 706 VAL TYR LEU GLN THR GLY GLU PRO LYS GLU LYS PHE LEU
SEQRES 21 A 706 THR ASN LEU SER TRP SER PRO ASP GLU ASN ILE LEU TYR
SEQRES 22 A 706 VAL ALA GLU VAL ASN ARG ALA GLN ASN GLU CYS LYS VAL
SEQRES 23 A 706 ASN ALA TYR ASP ALA GLU THR GLY ARG PHE VAL ARG THR
SEQRES 24 A 706 LEU PHE VAL GLU THR ASP LYS HIS TYR VAL GLU PRO LEU
SEQRES 25 A 706 HIS PRO LEU THR PHE LEU PRO GLY SER ASN ASN GLN PHE
SEQRES 26 A 706 ILE TRP GLN SER ARG ARG ASP GLY TRP ASN HIS LEU TYR
SEQRES 27 A 706 LEU TYR ASP THR THR GLY ARG LEU ILE ARG GLN VAL THR
SEQRES 28 A 706 LYS GLY GLU TRP GLU VAL THR ASN PHE ALA GLY PHE ASP
SEQRES 29 A 706 PRO LYS GLY THR ARG LEU TYR PHE GLU SER THR GLU ALA
SEQRES 30 A 706 SER PRO LEU GLU ARG HIS PHE TYR CYS ILE ASP ILE LYS
SEQRES 31 A 706 GLY GLY LYS THR LYS ASP LEU THR PRO GLU SER GLY MET
SEQRES 32 A 706 HIS ARG THR GLN LEU SER PRO ASP GLY SER ALA ILE ILE
SEQRES 33 A 706 ASP ILE PHE GLN SER PRO THR VAL PRO ARG LYS VAL THR
SEQRES 34 A 706 VAL THR ASN ILE GLY LYS GLY SER HIS THR LEU LEU GLU
SEQRES 35 A 706 ALA LYS ASN PRO ASP THR GLY TYR ALA MET PRO GLU ILE
SEQRES 36 A 706 ARG THR GLY THR ILE MET ALA ALA ASP GLY GLN THR PRO
SEQRES 37 A 706 LEU TYR TYR LYS LEU THR MET PRO LEU HIS PHE ASP PRO
SEQRES 38 A 706 ALA LYS LYS TYR PRO VAL ILE VAL TYR VAL TYR GLY GLY
SEQRES 39 A 706 PRO HIS ALA GLN LEU VAL THR LYS THR TRP ARG SER SER
SEQRES 40 A 706 VAL GLY GLY TRP ASP ILE TYR MET ALA GLN LYS GLY TYR
SEQRES 41 A 706 ALA VAL PHE THR VAL ASP SER ARG GLY SER ALA ASN ARG
SEQRES 42 A 706 GLY ALA ALA PHE GLU GLN VAL ILE HIS ARG ARG LEU GLY
SEQRES 43 A 706 GLN THR GLU MET ALA ASP GLN MET CYS GLY VAL ASP PHE
SEQRES 44 A 706 LEU LYS SER GLN SER TRP VAL ASP ALA ASP ARG ILE GLY
SEQRES 45 A 706 VAL HIS GLY TRP SER TYR GLY GLY PHE MET THR THR ASN
SEQRES 46 A 706 LEU MET LEU THR HIS GLY ASP VAL PHE LYS VAL GLY VAL
SEQRES 47 A 706 ALA GLY GLY PRO VAL ILE ASP TRP ASN ARG TYR ALA ILE
SEQRES 48 A 706 MET TYR GLY GLU ARG TYR PHE ASP ALA PRO GLN GLU ASN
SEQRES 49 A 706 PRO GLU GLY TYR ASP ALA ALA ASN LEU LEU LYS ARG ALA
SEQRES 50 A 706 GLY ASP LEU LYS GLY ARG LEU MET LEU ILE HIS GLY ALA
SEQRES 51 A 706 ILE ASP PRO VAL VAL VAL TRP GLN HIS SER LEU LEU PHE
SEQRES 52 A 706 LEU ASP ALA CYS VAL LYS ALA ARG THR TYR PRO ASP TYR
SEQRES 53 A 706 TYR VAL TYR PRO SER HIS GLU HIS ASN VAL MET GLY PRO
SEQRES 54 A 706 ASP ARG VAL HIS LEU TYR GLU THR ILE THR ARG TYR PHE
SEQRES 55 A 706 THR ASP HIS LEU
HET SO4 A 902 5
HET GOL A 901 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
FORMUL 2 SO4 O4 S 2-
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *547(H2 O)
HELIX 1 1 ALA A 89 MET A 96 1 8
HELIX 2 2 VAL A 201 GLU A 205 5 5
HELIX 3 3 GLY A 536 LYS A 544 1 9
HELIX 4 4 GLY A 560 VAL A 566 1 7
HELIX 5 5 GLY A 572 SER A 588 1 17
HELIX 6 6 SER A 603 HIS A 616 1 14
HELIX 7 7 ASP A 631 TYR A 635 5 5
HELIX 8 8 ALA A 636 ASP A 645 1 10
HELIX 9 9 ALA A 646 GLU A 649 5 4
HELIX 10 10 ASN A 650 ASN A 658 1 9
HELIX 11 11 LEU A 659 LEU A 666 5 8
HELIX 12 12 TRP A 683 ARG A 697 1 15
HELIX 13 13 PRO A 715 LEU A 732 1 18
SHEET 1 A 4 GLN A 58 MET A 60 0
SHEET 2 A 4 ASN A 63 GLU A 68 -1 O ASN A 63 N MET A 60
SHEET 3 A 4 ASP A 71 ASN A 75 -1 O VAL A 73 N PHE A 66
SHEET 4 A 4 THR A 85 SER A 88 -1 O THR A 85 N PHE A 74
SHEET 1 B 4 PHE A 111 ASP A 115 0
SHEET 2 B 4 LEU A 120 THR A 125 -1 O LEU A 120 N LEU A 114
SHEET 3 B 4 GLY A 128 ASP A 133 -1 O VAL A 130 N LEU A 123
SHEET 4 B 4 LYS A 138 PHE A 143 -1 O TYR A 141 N GLY A 131
SHEET 1 C 4 ASP A 153 PHE A 154 0
SHEET 2 C 4 ARG A 160 ARG A 165 -1 O ALA A 162 N ASP A 153
SHEET 3 C 4 ASN A 168 ARG A 173 -1 O ALA A 172 N VAL A 161
SHEET 4 C 4 ILE A 185 ALA A 186 -1 O ILE A 185 N ILE A 171
SHEET 1 D 3 LEU A 195 TYR A 197 0
SHEET 2 D 3 CYS A 220 ASP A 227 -1 O MET A 226 N VAL A 196
SHEET 3 D 3 THR A 212 TRP A 214 -1 N PHE A 213 O ALA A 222
SHEET 1 E 4 LEU A 195 TYR A 197 0
SHEET 2 E 4 CYS A 220 ASP A 227 -1 O MET A 226 N VAL A 196
SHEET 3 E 4 HIS A 260 HIS A 267 -1 O TYR A 266 N LEU A 221
SHEET 4 E 4 LYS A 272 TYR A 275 -1 O LYS A 272 N HIS A 267
SHEET 1 F 2 THR A 234 ASP A 238 0
SHEET 2 F 2 GLU A 245 LEU A 249 -1 O GLU A 245 N ASP A 238
SHEET 1 G 4 PHE A 285 TRP A 291 0
SHEET 2 G 4 ILE A 297 VAL A 303 -1 O TYR A 299 N SER A 290
SHEET 3 G 4 GLU A 309 ASP A 316 -1 O LYS A 311 N GLU A 302
SHEET 4 G 4 PHE A 322 THR A 330 -1 O LEU A 326 N VAL A 312
SHEET 1 H 4 THR A 342 PHE A 343 0
SHEET 2 H 4 GLN A 350 SER A 355 -1 O ILE A 352 N THR A 342
SHEET 3 H 4 HIS A 362 ASP A 367 -1 O TYR A 364 N TRP A 353
SHEET 4 H 4 LEU A 372 GLN A 375 -1 O ARG A 374 N LEU A 365
SHEET 1 I 4 VAL A 383 PHE A 389 0
SHEET 2 I 4 ARG A 395 SER A 400 -1 O TYR A 397 N GLY A 388
SHEET 3 I 4 HIS A 409 ASP A 414 -1 O TYR A 411 N PHE A 398
SHEET 4 I 4 LYS A 421 ASP A 422 -1 O LYS A 421 N CYS A 412
SHEET 1 J 4 MET A 429 LEU A 434 0
SHEET 2 J 4 ALA A 440 GLN A 446 -1 O GLN A 446 N MET A 429
SHEET 3 J 4 LYS A 453 ASN A 458 -1 O THR A 457 N ILE A 441
SHEET 4 J 4 SER A 463 GLU A 468 -1 O LEU A 466 N VAL A 454
SHEET 1 K 8 ILE A 481 MET A 487 0
SHEET 2 K 8 PRO A 494 THR A 500 -1 O LEU A 495 N ILE A 486
SHEET 3 K 8 ALA A 547 VAL A 551 -1 O VAL A 548 N THR A 500
SHEET 4 K 8 TYR A 511 TYR A 516 1 N ILE A 514 O ALA A 547
SHEET 5 K 8 VAL A 592 TRP A 602 1 O GLY A 598 N VAL A 515
SHEET 6 K 8 PHE A 620 GLY A 626 1 O LYS A 621 N ILE A 597
SHEET 7 K 8 ARG A 669 GLY A 675 1 O ARG A 669 N GLY A 623
SHEET 8 K 8 ASP A 701 TYR A 705 1 O ASP A 701 N LEU A 670
CISPEP 1 GLU A 280 PRO A 281 0 -3.26
CISPEP 2 GLY A 460 LYS A 461 0 3.71
SITE 1 AC1 5 ARG A 321 SER A 347 ASN A 349 GLN A 350
SITE 2 AC1 5 HOH A1048
SITE 1 AC2 6 TYR A 518 SER A 603 TYR A 604 TYR A 635
SITE 2 AC2 6 TYR A 639 HOH A1030
CRYST1 149.709 149.709 160.943 90.00 90.00 120.00 P 63 2 2 12
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 0.006680 0.003856 0.000000 0.00000
SCALE2 0.000000 0.007713 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006213 0.00000
TER 5194 LEU A 732
MASTER 406 0 2 13 45 0 4 6 5751 1 11 55
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