HEADER LYASE 17-OCT-13 3WK1
TITLE WILD-TYPE OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM M.
TITLE 2 THERMOAUTOTROPHICUS COMPLEXED WITH OROTIDINE 5'-MONOPHOSPHATE ETHYL
TITLE 3 ESTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OROTIDINE 5'-PHOSPHATE DECARBOXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OMP DECARBOXYLASE, OMPDCASE, OMPDECASE;
COMPND 5 EC: 4.1.1.23;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 145262;
SOURCE 4 STRAIN: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / DELTA H;
SOURCE 5 GENE: PYRF, MTH_129;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS PROTEIN-LIGAND COMPLEX, TIM BARREL, DECARBOXYLASE, PYRIMIDINE
KEYWDS 2 BIOSYNTHESIS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FUJIHASHI,E.F.PAI,K.MIKI
REVDAT 2 08-NOV-23 3WK1 1 REMARK SEQADV
REVDAT 1 04-DEC-13 3WK1 0
JRNL AUTH M.FUJIHASHI,T.ISHIDA,S.KURODA,L.P.KOTRA,E.F.PAI,K.MIKI
JRNL TITL SUBSTRATE DISTORTION CONTRIBUTES TO THE CATALYSIS OF
JRNL TITL 2 OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE.
JRNL REF J.AM.CHEM.SOC. V. 135 17432 2013
JRNL REFN ISSN 0002-7863
JRNL PMID 24151964
JRNL DOI 10.1021/JA408197K
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 29436
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1468
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2020
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.1730
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.2100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1630
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 168
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.42000
REMARK 3 B22 (A**2) : -0.84000
REMARK 3 B33 (A**2) : 0.42000
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): 0.088
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.081
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.043
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.593
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
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): 1969 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2682 ; 1.630 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 263 ; 5.747 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;36.229 ;22.747
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 351 ;13.645 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;20.578 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 292 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1544 ; 0.010 ; 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): 1225 ; 0.889 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1995 ; 1.520 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 744 ; 2.770 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 686 ; 4.461 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 11 A 225
REMARK 3 RESIDUE RANGE : A 301 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5950 40.4939 29.6907
REMARK 3 T TENSOR
REMARK 3 T11: 0.0278 T22: 0.0170
REMARK 3 T33: 0.0091 T12: 0.0027
REMARK 3 T13: -0.0065 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.4676 L22: 0.8882
REMARK 3 L33: 0.4957 L12: -0.0659
REMARK 3 L13: -0.0162 L23: -0.1918
REMARK 3 S TENSOR
REMARK 3 S11: 0.0139 S12: 0.0411 S13: -0.0510
REMARK 3 S21: -0.1153 S22: 0.0107 S23: 0.0019
REMARK 3 S31: 0.0873 S32: 0.0030 S33: -0.0246
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 3WK1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000096432.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : APS
REMARK 200 BEAMLINE : 14-BM-D
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 : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30030
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.590
REMARK 200 RESOLUTION RANGE LOW (A) : 51.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 38.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.29800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5
REMARK 200 STARTING MODEL: 3WK3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PH 8.5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.79500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.79500
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 28.90000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.74500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 28.90000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.74500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.79500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 28.90000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.74500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 36.79500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 28.90000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.74500
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 103.49000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 73.59000
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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 SER A 3
REMARK 465 ARG A 4
REMARK 465 ARG A 5
REMARK 465 VAL A 6
REMARK 465 ASP A 7
REMARK 465 VAL A 8
REMARK 465 MET A 9
REMARK 465 ASP A 10
REMARK 465 ARG A 226
REMARK 465 ILE A 227
REMARK 465 PRO A 228
REMARK 465 GLU A 229
REMARK 465 ASP A 230
REMARK 465 PRO A 231
REMARK 465 ALA A 232
REMARK 465 ALA A 233
REMARK 465 ASN A 234
REMARK 465 LYS A 235
REMARK 465 ALA A 236
REMARK 465 ARG A 237
REMARK 465 LYS A 238
REMARK 465 GLU A 239
REMARK 465 ALA A 240
REMARK 465 GLU A 241
REMARK 465 LEU A 242
REMARK 465 ALA A 243
REMARK 465 ALA A 244
REMARK 465 ALA A 245
REMARK 465 THR A 246
REMARK 465 ALA A 247
REMARK 465 GLU A 248
REMARK 465 GLN A 249
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 ALA A 74 43.48 -151.69
REMARK 500 THR A 124 -91.01 -91.64
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 O7E A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WJW RELATED DB: PDB
REMARK 900 RELATED ID: 3WJX RELATED DB: PDB
REMARK 900 RELATED ID: 3WJY RELATED DB: PDB
REMARK 900 RELATED ID: 3WKZ RELATED DB: PDB
REMARK 900 RELATED ID: 3WK0 RELATED DB: PDB
REMARK 900 RELATED ID: 3WK2 RELATED DB: PDB
REMARK 900 RELATED ID: 3WK3 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ACCORDING TO DEPOSITORS, PRO101 IS CORRECT AND UNIPORT IS PROBABLY
REMARK 999 INCORRECT AT THIS POSITION. DEPOSITORS SEQUENCED THE GENOME FROM M.
REMARK 999 THERMOAUTOTROPHICUS AND CONFIRMED IT IS PRO.
DBREF 3WK1 A 1 228 UNP O26232 PYRF_METTH 1 228
SEQADV 3WK1 GLY A -2 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 SER A -1 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 HIS A 0 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 PRO A 101 UNP O26232 ARG 101 SEE REMARK 999
SEQADV 3WK1 ARG A 226 UNP O26232 LEU 226 ENGINEERED MUTATION
SEQADV 3WK1 ILE A 227 UNP O26232 ASN 227 ENGINEERED MUTATION
SEQADV 3WK1 GLU A 229 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ASP A 230 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 PRO A 231 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ALA A 232 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ALA A 233 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ASN A 234 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 LYS A 235 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ALA A 236 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ARG A 237 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 LYS A 238 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 GLU A 239 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ALA A 240 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 GLU A 241 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 LEU A 242 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ALA A 243 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ALA A 244 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ALA A 245 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 THR A 246 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 ALA A 247 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 GLU A 248 UNP O26232 EXPRESSION TAG
SEQADV 3WK1 GLN A 249 UNP O26232 EXPRESSION TAG
SEQRES 1 A 252 GLY SER HIS MET ARG SER ARG ARG VAL ASP VAL MET ASP
SEQRES 2 A 252 VAL MET ASN ARG LEU ILE LEU ALA MET ASP LEU MET ASN
SEQRES 3 A 252 ARG ASP ASP ALA LEU ARG VAL THR GLY GLU VAL ARG GLU
SEQRES 4 A 252 TYR ILE ASP THR VAL LYS ILE GLY TYR PRO LEU VAL LEU
SEQRES 5 A 252 SER GLU GLY MET ASP ILE ILE ALA GLU PHE ARG LYS ARG
SEQRES 6 A 252 PHE GLY CYS ARG ILE ILE ALA ASP PHE LYS VAL ALA ASP
SEQRES 7 A 252 ILE PRO GLU THR ASN GLU LYS ILE CYS ARG ALA THR PHE
SEQRES 8 A 252 LYS ALA GLY ALA ASP ALA ILE ILE VAL HIS GLY PHE PRO
SEQRES 9 A 252 GLY ALA ASP SER VAL ARG ALA CYS LEU ASN VAL ALA GLU
SEQRES 10 A 252 GLU MET GLY ARG GLU VAL PHE LEU LEU THR GLU MET SER
SEQRES 11 A 252 HIS PRO GLY ALA GLU MET PHE ILE GLN GLY ALA ALA ASP
SEQRES 12 A 252 GLU ILE ALA ARG MET GLY VAL ASP LEU GLY VAL LYS ASN
SEQRES 13 A 252 TYR VAL GLY PRO SER THR ARG PRO GLU ARG LEU SER ARG
SEQRES 14 A 252 LEU ARG GLU ILE ILE GLY GLN ASP SER PHE LEU ILE SER
SEQRES 15 A 252 PRO GLY VAL GLY ALA GLN GLY GLY ASP PRO GLY GLU THR
SEQRES 16 A 252 LEU ARG PHE ALA ASP ALA ILE ILE VAL GLY ARG SER ILE
SEQRES 17 A 252 TYR LEU ALA ASP ASN PRO ALA ALA ALA ALA ALA GLY ILE
SEQRES 18 A 252 ILE GLU SER ILE LYS ASP LEU ARG ILE PRO GLU ASP PRO
SEQRES 19 A 252 ALA ALA ASN LYS ALA ARG LYS GLU ALA GLU LEU ALA ALA
SEQRES 20 A 252 ALA THR ALA GLU GLN
HET O7E A 301 26
HET GOL A 302 6
HET GOL A 303 6
HETNAM O7E 6-(ETHOXYCARBONYL)URIDINE 5'-(DIHYDROGEN PHOSPHATE)
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 O7E C12 H17 N2 O11 P
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *168(H2 O)
HELIX 1 1 VAL A 11 ASN A 13 5 3
HELIX 2 2 ASN A 23 ARG A 35 1 13
HELIX 3 3 GLU A 36 ILE A 38 5 3
HELIX 4 4 TYR A 45 GLY A 52 1 8
HELIX 5 5 MET A 53 GLY A 64 1 12
HELIX 6 6 ILE A 76 ALA A 90 1 15
HELIX 7 7 GLY A 102 GLY A 117 1 16
HELIX 8 8 HIS A 128 MET A 133 5 6
HELIX 9 9 PHE A 134 GLY A 150 1 17
HELIX 10 10 ARG A 160 GLY A 172 1 13
HELIX 11 11 ASP A 188 LEU A 193 1 6
HELIX 12 12 GLY A 202 LEU A 207 1 6
HELIX 13 13 ASN A 210 LEU A 225 1 16
SHEET 1 A 9 LEU A 15 MET A 19 0
SHEET 2 A 9 THR A 40 GLY A 44 1 O LYS A 42 N LEU A 17
SHEET 3 A 9 ARG A 66 VAL A 73 1 O ARG A 66 N VAL A 41
SHEET 4 A 9 ALA A 94 HIS A 98 1 O ALA A 94 N ALA A 69
SHEET 5 A 9 GLU A 119 LEU A 123 1 O LEU A 123 N VAL A 97
SHEET 6 A 9 ASN A 153 VAL A 155 1 O ASN A 153 N LEU A 122
SHEET 7 A 9 PHE A 176 SER A 179 1 O ILE A 178 N TYR A 154
SHEET 8 A 9 ALA A 198 VAL A 201 1 O ILE A 200 N SER A 179
SHEET 9 A 9 LEU A 15 MET A 19 1 N ILE A 16 O ILE A 199
SITE 1 AC1 20 ASP A 20 LYS A 42 ASP A 70 LYS A 72
SITE 2 AC1 20 ASP A 75 ILE A 76 THR A 79 LEU A 123
SITE 3 AC1 20 MET A 126 SER A 127 PRO A 180 GLN A 185
SITE 4 AC1 20 GLY A 202 ARG A 203 HOH A 402 HOH A 403
SITE 5 AC1 20 HOH A 406 HOH A 407 HOH A 408 HOH A 411
SITE 1 AC2 7 THR A 159 PRO A 161 GLY A 186 ASN A 210
SITE 2 AC2 7 HOH A 421 HOH A 429 HOH A 549
SITE 1 AC3 7 GLU A 162 ALA A 208 ASP A 209 ASN A 210
SITE 2 AC3 7 ALA A 213 ALA A 214 HOH A 433
CRYST1 57.800 103.490 73.590 90.00 90.00 90.00 C 2 2 21 8
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 0.017301 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013589 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
