HEADER LYASE 05-JAN-00 1DQW
TITLE CRYSTAL STRUCTURE OF OROTIDINE 5'-PHOSPHATE DECARBOXYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OROTIDINE 5'-PHOSPHATE DECARBOXYLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 4.1.1.23;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCDA6022
KEYWDS TIM BARREL, OROTIDINE 5'-PHOSPHATE, URIDINE 5'-PHOSPHATE,
KEYWDS 2 DECARBOXYLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.V.MILBURN,B.G.MILLER,A.M.HASSELL,R.WOLFENDEN,S.A.SHORT
REVDAT 2 24-FEB-09 1DQW 1 VERSN
REVDAT 1 20-MAR-00 1DQW 0
JRNL AUTH B.G.MILLER,A.M.HASSELL,R.WOLFENDEN,M.V.MILBURN,
JRNL AUTH 2 S.A.SHORT
JRNL TITL ANATOMY OF A PROFICIENT ENZYME: THE STRUCTURE OF
JRNL TITL 2 OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE IN THE
JRNL TITL 3 PRESENCE AND ABSENCE OF A POTENTIAL TRANSITION
JRNL TITL 4 STATE ANALOG.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 2011 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 10681417
JRNL DOI 10.1073/PNAS.030409797
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2473075.210
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.1
REMARK 3 NUMBER OF REFLECTIONS : 65044
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) : 0.218
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.200
REMARK 3 FREE R VALUE TEST SET COUNT : 5311
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4889
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 452
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8236
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 874
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.44000
REMARK 3 B22 (A**2) : -0.35000
REMARK 3 B33 (A**2) : -3.09000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 2.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.93
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.940 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.880 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.800 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 85.65
REMARK 3
REMARK 3 NCS MODEL : CONSTRAINED
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DQW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-00.
REMARK 100 THE RCSB ID CODE IS RCSB010308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-99
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0281
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70148
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 97.1
REMARK 200 DATA REDUNDANCY : 15.100
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 9.00
REMARK 200 R MERGE FOR SHELL (I) : 0.11300
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: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM-HEPES, ISOPROPANOL,
REMARK 280 POLYETHYLENE GLYCOL 4000, PH 7.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 278.0K
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 45.03000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.48950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.10850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.48950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.03000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.10850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER OF MOLECULE A RELATED
REMARK 300 BY A TWO-FOLD SYMMETRY AXIS TO MOLECULE B, OR MOLECULE C RELATED
REMARK 300 BY A TWO-FOLD SYMMETRY AXIS TO MOLECULE D.
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: 2930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 2940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 217 C ARG A 218 N -0.170
REMARK 500 TYR B 217 C ARG B 218 N -0.168
REMARK 500 TYR C 217 C ARG C 218 N -0.217
REMARK 500 TYR D 217 C ARG D 218 N -0.158
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 GLY A 205 CA - C - N ANGL. DEV. = -15.9 DEGREES
REMARK 500 GLY A 205 O - C - N ANGL. DEV. = -101.7 DEGREES
REMARK 500 TYR A 217 CA - C - N ANGL. DEV. = 14.5 DEGREES
REMARK 500 TYR A 217 O - C - N ANGL. DEV. = -14.7 DEGREES
REMARK 500 ARG A 218 C - N - CA ANGL. DEV. = 17.2 DEGREES
REMARK 500 GLY B 205 CA - C - N ANGL. DEV. = -20.5 DEGREES
REMARK 500 GLY B 205 O - C - N ANGL. DEV. = -96.3 DEGREES
REMARK 500 LEU B 206 C - N - CA ANGL. DEV. = -16.7 DEGREES
REMARK 500 TYR B 217 CA - C - N ANGL. DEV. = 21.1 DEGREES
REMARK 500 TYR B 217 O - C - N ANGL. DEV. = -22.0 DEGREES
REMARK 500 ARG B 218 C - N - CA ANGL. DEV. = 25.7 DEGREES
REMARK 500 GLY C 205 CA - C - N ANGL. DEV. = -16.9 DEGREES
REMARK 500 GLY C 205 O - C - N ANGL. DEV. = -101.6 DEGREES
REMARK 500 TYR C 217 CA - C - N ANGL. DEV. = 15.8 DEGREES
REMARK 500 TYR C 217 O - C - N ANGL. DEV. = -16.6 DEGREES
REMARK 500 ARG C 218 C - N - CA ANGL. DEV. = 20.1 DEGREES
REMARK 500 GLY D 205 CA - C - N ANGL. DEV. = -19.7 DEGREES
REMARK 500 GLY D 205 O - C - N ANGL. DEV. = -99.1 DEGREES
REMARK 500 LEU D 206 C - N - CA ANGL. DEV. = -15.0 DEGREES
REMARK 500 TYR D 217 CA - C - N ANGL. DEV. = 17.6 DEGREES
REMARK 500 TYR D 217 O - C - N ANGL. DEV. = -17.9 DEGREES
REMARK 500 ARG D 218 C - N - CA ANGL. DEV. = 20.7 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 HIS A 2 -163.77 -73.35
REMARK 500 ASN A 85 75.18 60.26
REMARK 500 ALA A 95 57.57 -145.11
REMARK 500 ALA A 107 -137.73 -126.76
REMARK 500 ASP A 175 116.54 -173.82
REMARK 500 ASP A 196 78.86 -119.61
REMARK 500 GLN A 215 52.05 77.14
REMARK 500 TYR A 217 -33.48 -146.32
REMARK 500 PHE A 238 -11.29 -140.95
REMARK 500 LYS A 240 78.69 25.99
REMARK 500 GLN A 266 -27.25 -152.53
REMARK 500 LEU B 36 79.89 -106.90
REMARK 500 ASP B 67 47.77 -142.87
REMARK 500 ASN B 85 72.41 53.27
REMARK 500 ALA B 95 56.38 -144.24
REMARK 500 ALA B 107 -140.47 -132.14
REMARK 500 ASP B 175 118.81 -174.85
REMARK 500 GLN B 215 50.95 78.75
REMARK 500 TYR B 217 -36.74 -149.47
REMARK 500 PHE B 238 -7.12 -140.89
REMARK 500 LYS B 240 76.94 30.56
REMARK 500 GLN B 266 -27.26 -151.63
REMARK 500 HIS C 2 -165.52 -73.31
REMARK 500 ASP C 67 45.51 -143.91
REMARK 500 ASN C 85 74.50 61.70
REMARK 500 ALA C 95 56.94 -147.46
REMARK 500 ALA C 107 -136.09 -124.08
REMARK 500 ASP C 175 119.59 -172.48
REMARK 500 GLN C 215 51.12 76.84
REMARK 500 TYR C 217 -27.70 -144.21
REMARK 500 PHE C 238 -8.95 -142.75
REMARK 500 LYS C 240 73.21 32.32
REMARK 500 GLN C 266 -22.41 -154.11
REMARK 500 ASP D 67 49.11 -142.06
REMARK 500 ASN D 85 72.92 58.16
REMARK 500 ALA D 95 55.33 -144.32
REMARK 500 ALA D 107 -136.63 -131.61
REMARK 500 ASP D 175 115.79 -177.01
REMARK 500 ASP D 196 79.59 -119.63
REMARK 500 GLN D 215 55.83 74.37
REMARK 500 TYR D 217 -29.42 -145.89
REMARK 500 PHE D 238 -6.87 -143.21
REMARK 500 LYS D 240 74.85 26.84
REMARK 500 GLN D 266 -27.16 -154.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A 205 -16.48
REMARK 500 GLY B 205 -16.81
REMARK 500 GLY C 205 -12.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 398 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH C 414 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH A 416 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH D 440 DISTANCE = 5.29 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DQX RELATED DB: PDB
REMARK 900 1DQX IS THE CRYSTAL STRUCTURE OF THE SAME PROTEIN COMPLEXED
REMARK 900 WITH 6-HYDROXYURIDINE 5'PHOSPHATE.
DBREF 1DQW A 1 267 UNP P03962 PYRF_YEAST 1 267
DBREF 1DQW B 1 267 UNP P03962 PYRF_YEAST 1 267
DBREF 1DQW C 1 267 UNP P03962 PYRF_YEAST 1 267
DBREF 1DQW D 1 267 UNP P03962 PYRF_YEAST 1 267
SEQADV 1DQW HIS A 2 UNP P03962 SER 2 ENGINEERED
SEQADV 1DQW ASP A 267 UNP P03962 ASN 267 ENGINEERED
SEQADV 1DQW HIS B 2 UNP P03962 SER 2 ENGINEERED
SEQADV 1DQW ASP B 267 UNP P03962 ASN 267 ENGINEERED
SEQADV 1DQW HIS C 2 UNP P03962 SER 2 ENGINEERED
SEQADV 1DQW ASP C 267 UNP P03962 ASN 267 ENGINEERED
SEQADV 1DQW HIS D 2 UNP P03962 SER 2 ENGINEERED
SEQADV 1DQW ASP D 267 UNP P03962 ASN 267 ENGINEERED
SEQRES 1 A 267 MET HIS LYS ALA THR TYR LYS GLU ARG ALA ALA THR HIS
SEQRES 2 A 267 PRO SER PRO VAL ALA ALA LYS LEU PHE ASN ILE MET HIS
SEQRES 3 A 267 GLU LYS GLN THR ASN LEU CYS ALA SER LEU ASP VAL ARG
SEQRES 4 A 267 THR THR LYS GLU LEU LEU GLU LEU VAL GLU ALA LEU GLY
SEQRES 5 A 267 PRO LYS ILE CYS LEU LEU LYS THR HIS VAL ASP ILE LEU
SEQRES 6 A 267 THR ASP PHE SER MET GLU GLY THR VAL LYS PRO LEU LYS
SEQRES 7 A 267 ALA LEU SER ALA LYS TYR ASN PHE LEU LEU PHE GLU ASP
SEQRES 8 A 267 ARG LYS PHE ALA ASP ILE GLY ASN THR VAL LYS LEU GLN
SEQRES 9 A 267 TYR SER ALA GLY VAL TYR ARG ILE ALA GLU TRP ALA ASP
SEQRES 10 A 267 ILE THR ASN ALA HIS GLY VAL VAL GLY PRO GLY ILE VAL
SEQRES 11 A 267 SER GLY LEU LYS GLN ALA ALA GLU GLU VAL THR LYS GLU
SEQRES 12 A 267 PRO ARG GLY LEU LEU MET LEU ALA GLU LEU SER CYS LYS
SEQRES 13 A 267 GLY SER LEU SER THR GLY GLU TYR THR LYS GLY THR VAL
SEQRES 14 A 267 ASP ILE ALA LYS SER ASP LYS ASP PHE VAL ILE GLY PHE
SEQRES 15 A 267 ILE ALA GLN ARG ASP MET GLY GLY ARG ASP GLU GLY TYR
SEQRES 16 A 267 ASP TRP LEU ILE MET THR PRO GLY VAL GLY LEU ASP ASP
SEQRES 17 A 267 LYS GLY ASP ALA LEU GLY GLN GLN TYR ARG THR VAL ASP
SEQRES 18 A 267 ASP VAL VAL SER THR GLY SER ASP ILE ILE ILE VAL GLY
SEQRES 19 A 267 ARG GLY LEU PHE ALA LYS GLY ARG ASP ALA LYS VAL GLU
SEQRES 20 A 267 GLY GLU ARG TYR ARG LYS ALA GLY TRP GLU ALA TYR LEU
SEQRES 21 A 267 ARG ARG CYS GLY GLN GLN ASP
SEQRES 1 B 267 MET HIS LYS ALA THR TYR LYS GLU ARG ALA ALA THR HIS
SEQRES 2 B 267 PRO SER PRO VAL ALA ALA LYS LEU PHE ASN ILE MET HIS
SEQRES 3 B 267 GLU LYS GLN THR ASN LEU CYS ALA SER LEU ASP VAL ARG
SEQRES 4 B 267 THR THR LYS GLU LEU LEU GLU LEU VAL GLU ALA LEU GLY
SEQRES 5 B 267 PRO LYS ILE CYS LEU LEU LYS THR HIS VAL ASP ILE LEU
SEQRES 6 B 267 THR ASP PHE SER MET GLU GLY THR VAL LYS PRO LEU LYS
SEQRES 7 B 267 ALA LEU SER ALA LYS TYR ASN PHE LEU LEU PHE GLU ASP
SEQRES 8 B 267 ARG LYS PHE ALA ASP ILE GLY ASN THR VAL LYS LEU GLN
SEQRES 9 B 267 TYR SER ALA GLY VAL TYR ARG ILE ALA GLU TRP ALA ASP
SEQRES 10 B 267 ILE THR ASN ALA HIS GLY VAL VAL GLY PRO GLY ILE VAL
SEQRES 11 B 267 SER GLY LEU LYS GLN ALA ALA GLU GLU VAL THR LYS GLU
SEQRES 12 B 267 PRO ARG GLY LEU LEU MET LEU ALA GLU LEU SER CYS LYS
SEQRES 13 B 267 GLY SER LEU SER THR GLY GLU TYR THR LYS GLY THR VAL
SEQRES 14 B 267 ASP ILE ALA LYS SER ASP LYS ASP PHE VAL ILE GLY PHE
SEQRES 15 B 267 ILE ALA GLN ARG ASP MET GLY GLY ARG ASP GLU GLY TYR
SEQRES 16 B 267 ASP TRP LEU ILE MET THR PRO GLY VAL GLY LEU ASP ASP
SEQRES 17 B 267 LYS GLY ASP ALA LEU GLY GLN GLN TYR ARG THR VAL ASP
SEQRES 18 B 267 ASP VAL VAL SER THR GLY SER ASP ILE ILE ILE VAL GLY
SEQRES 19 B 267 ARG GLY LEU PHE ALA LYS GLY ARG ASP ALA LYS VAL GLU
SEQRES 20 B 267 GLY GLU ARG TYR ARG LYS ALA GLY TRP GLU ALA TYR LEU
SEQRES 21 B 267 ARG ARG CYS GLY GLN GLN ASP
SEQRES 1 C 267 MET HIS LYS ALA THR TYR LYS GLU ARG ALA ALA THR HIS
SEQRES 2 C 267 PRO SER PRO VAL ALA ALA LYS LEU PHE ASN ILE MET HIS
SEQRES 3 C 267 GLU LYS GLN THR ASN LEU CYS ALA SER LEU ASP VAL ARG
SEQRES 4 C 267 THR THR LYS GLU LEU LEU GLU LEU VAL GLU ALA LEU GLY
SEQRES 5 C 267 PRO LYS ILE CYS LEU LEU LYS THR HIS VAL ASP ILE LEU
SEQRES 6 C 267 THR ASP PHE SER MET GLU GLY THR VAL LYS PRO LEU LYS
SEQRES 7 C 267 ALA LEU SER ALA LYS TYR ASN PHE LEU LEU PHE GLU ASP
SEQRES 8 C 267 ARG LYS PHE ALA ASP ILE GLY ASN THR VAL LYS LEU GLN
SEQRES 9 C 267 TYR SER ALA GLY VAL TYR ARG ILE ALA GLU TRP ALA ASP
SEQRES 10 C 267 ILE THR ASN ALA HIS GLY VAL VAL GLY PRO GLY ILE VAL
SEQRES 11 C 267 SER GLY LEU LYS GLN ALA ALA GLU GLU VAL THR LYS GLU
SEQRES 12 C 267 PRO ARG GLY LEU LEU MET LEU ALA GLU LEU SER CYS LYS
SEQRES 13 C 267 GLY SER LEU SER THR GLY GLU TYR THR LYS GLY THR VAL
SEQRES 14 C 267 ASP ILE ALA LYS SER ASP LYS ASP PHE VAL ILE GLY PHE
SEQRES 15 C 267 ILE ALA GLN ARG ASP MET GLY GLY ARG ASP GLU GLY TYR
SEQRES 16 C 267 ASP TRP LEU ILE MET THR PRO GLY VAL GLY LEU ASP ASP
SEQRES 17 C 267 LYS GLY ASP ALA LEU GLY GLN GLN TYR ARG THR VAL ASP
SEQRES 18 C 267 ASP VAL VAL SER THR GLY SER ASP ILE ILE ILE VAL GLY
SEQRES 19 C 267 ARG GLY LEU PHE ALA LYS GLY ARG ASP ALA LYS VAL GLU
SEQRES 20 C 267 GLY GLU ARG TYR ARG LYS ALA GLY TRP GLU ALA TYR LEU
SEQRES 21 C 267 ARG ARG CYS GLY GLN GLN ASP
SEQRES 1 D 267 MET HIS LYS ALA THR TYR LYS GLU ARG ALA ALA THR HIS
SEQRES 2 D 267 PRO SER PRO VAL ALA ALA LYS LEU PHE ASN ILE MET HIS
SEQRES 3 D 267 GLU LYS GLN THR ASN LEU CYS ALA SER LEU ASP VAL ARG
SEQRES 4 D 267 THR THR LYS GLU LEU LEU GLU LEU VAL GLU ALA LEU GLY
SEQRES 5 D 267 PRO LYS ILE CYS LEU LEU LYS THR HIS VAL ASP ILE LEU
SEQRES 6 D 267 THR ASP PHE SER MET GLU GLY THR VAL LYS PRO LEU LYS
SEQRES 7 D 267 ALA LEU SER ALA LYS TYR ASN PHE LEU LEU PHE GLU ASP
SEQRES 8 D 267 ARG LYS PHE ALA ASP ILE GLY ASN THR VAL LYS LEU GLN
SEQRES 9 D 267 TYR SER ALA GLY VAL TYR ARG ILE ALA GLU TRP ALA ASP
SEQRES 10 D 267 ILE THR ASN ALA HIS GLY VAL VAL GLY PRO GLY ILE VAL
SEQRES 11 D 267 SER GLY LEU LYS GLN ALA ALA GLU GLU VAL THR LYS GLU
SEQRES 12 D 267 PRO ARG GLY LEU LEU MET LEU ALA GLU LEU SER CYS LYS
SEQRES 13 D 267 GLY SER LEU SER THR GLY GLU TYR THR LYS GLY THR VAL
SEQRES 14 D 267 ASP ILE ALA LYS SER ASP LYS ASP PHE VAL ILE GLY PHE
SEQRES 15 D 267 ILE ALA GLN ARG ASP MET GLY GLY ARG ASP GLU GLY TYR
SEQRES 16 D 267 ASP TRP LEU ILE MET THR PRO GLY VAL GLY LEU ASP ASP
SEQRES 17 D 267 LYS GLY ASP ALA LEU GLY GLN GLN TYR ARG THR VAL ASP
SEQRES 18 D 267 ASP VAL VAL SER THR GLY SER ASP ILE ILE ILE VAL GLY
SEQRES 19 D 267 ARG GLY LEU PHE ALA LYS GLY ARG ASP ALA LYS VAL GLU
SEQRES 20 D 267 GLY GLU ARG TYR ARG LYS ALA GLY TRP GLU ALA TYR LEU
SEQRES 21 D 267 ARG ARG CYS GLY GLN GLN ASP
FORMUL 5 HOH *874(H2 O)
HELIX 1 1 THR A 5 HIS A 13 1 9
HELIX 2 2 SER A 15 GLN A 29 1 15
HELIX 3 3 THR A 40 GLY A 52 1 13
HELIX 4 4 PRO A 53 ILE A 55 5 3
HELIX 5 5 HIS A 61 LEU A 65 5 5
HELIX 6 6 THR A 73 ASN A 85 1 13
HELIX 7 7 ILE A 97 ALA A 107 1 11
HELIX 8 8 ARG A 111 ALA A 116 1 6
HELIX 9 9 PRO A 127 THR A 141 1 15
HELIX 10 10 THR A 161 LYS A 173 1 13
HELIX 11 11 THR A 219 THR A 226 1 8
HELIX 12 12 GLY A 234 PHE A 238 5 5
HELIX 13 13 ASP A 243 GLY A 264 1 22
HELIX 14 14 THR B 5 HIS B 13 1 9
HELIX 15 15 SER B 15 GLN B 29 1 15
HELIX 16 16 THR B 40 GLY B 52 1 13
HELIX 17 17 PRO B 53 ILE B 55 5 3
HELIX 18 18 HIS B 61 LEU B 65 5 5
HELIX 19 19 THR B 73 TYR B 84 1 12
HELIX 20 20 ILE B 97 ALA B 107 1 11
HELIX 21 21 ARG B 111 TRP B 115 5 5
HELIX 22 22 PRO B 127 THR B 141 1 15
HELIX 23 23 THR B 161 LYS B 173 1 13
HELIX 24 24 GLY B 190 GLY B 194 5 5
HELIX 25 25 THR B 219 THR B 226 1 8
HELIX 26 26 GLY B 234 PHE B 238 5 5
HELIX 27 27 ASP B 243 CYS B 263 1 21
HELIX 28 28 THR C 5 HIS C 13 1 9
HELIX 29 29 SER C 15 GLN C 29 1 15
HELIX 30 30 THR C 40 GLY C 52 1 13
HELIX 31 31 PRO C 53 ILE C 55 5 3
HELIX 32 32 HIS C 61 LEU C 65 5 5
HELIX 33 33 THR C 73 ASN C 85 1 13
HELIX 34 34 ILE C 97 ALA C 107 1 11
HELIX 35 35 ARG C 111 ALA C 116 1 6
HELIX 36 36 PRO C 127 THR C 141 1 15
HELIX 37 37 THR C 161 LYS C 173 1 13
HELIX 38 38 GLY C 190 GLY C 194 5 5
HELIX 39 39 THR C 219 THR C 226 1 8
HELIX 40 40 GLY C 234 PHE C 238 5 5
HELIX 41 41 ASP C 243 GLY C 264 1 22
HELIX 42 42 THR D 5 HIS D 13 1 9
HELIX 43 43 SER D 15 GLN D 29 1 15
HELIX 44 44 THR D 40 GLY D 52 1 13
HELIX 45 45 PRO D 53 ILE D 55 5 3
HELIX 46 46 HIS D 61 LEU D 65 5 5
HELIX 47 47 THR D 73 ASN D 85 1 13
HELIX 48 48 ILE D 97 ALA D 107 1 11
HELIX 49 49 ARG D 111 ALA D 116 1 6
HELIX 50 50 PRO D 127 THR D 141 1 15
HELIX 51 51 THR D 161 LYS D 173 1 13
HELIX 52 52 THR D 219 THR D 226 1 8
HELIX 53 53 GLY D 234 PHE D 238 5 5
HELIX 54 54 ASP D 243 CYS D 263 1 21
SHEET 1 A 9 LEU A 32 SER A 35 0
SHEET 2 A 9 LEU A 57 THR A 60 1 O LEU A 57 N ALA A 34
SHEET 3 A 9 LEU A 87 PHE A 94 1 O LEU A 87 N LEU A 58
SHEET 4 A 9 ILE A 118 HIS A 122 1 N ILE A 118 O LEU A 88
SHEET 5 A 9 GLY A 146 LEU A 150 1 O GLY A 146 N THR A 119
SHEET 6 A 9 VAL A 179 ILE A 183 1 N ILE A 180 O LEU A 147
SHEET 7 A 9 LEU A 198 THR A 201 1 N LEU A 198 O ILE A 180
SHEET 8 A 9 ILE A 230 VAL A 233 1 O ILE A 230 N THR A 201
SHEET 9 A 9 LEU A 32 SER A 35 1 N CYS A 33 O ILE A 231
SHEET 1 B 9 LEU B 32 SER B 35 0
SHEET 2 B 9 LEU B 57 THR B 60 1 O LEU B 57 N ALA B 34
SHEET 3 B 9 LEU B 87 PHE B 94 1 O LEU B 87 N LEU B 58
SHEET 4 B 9 ILE B 118 HIS B 122 1 N ILE B 118 O LEU B 88
SHEET 5 B 9 GLY B 146 LEU B 150 1 O GLY B 146 N THR B 119
SHEET 6 B 9 VAL B 179 ILE B 183 1 N ILE B 180 O LEU B 147
SHEET 7 B 9 LEU B 198 THR B 201 1 N LEU B 198 O ILE B 180
SHEET 8 B 9 ILE B 230 VAL B 233 1 O ILE B 230 N THR B 201
SHEET 9 B 9 LEU B 32 SER B 35 1 N CYS B 33 O ILE B 231
SHEET 1 C 9 LEU C 32 SER C 35 0
SHEET 2 C 9 LEU C 57 THR C 60 1 O LEU C 57 N ALA C 34
SHEET 3 C 9 LEU C 87 PHE C 94 1 O LEU C 87 N LEU C 58
SHEET 4 C 9 ILE C 118 HIS C 122 1 N ILE C 118 O LEU C 88
SHEET 5 C 9 GLY C 146 LEU C 150 1 O GLY C 146 N THR C 119
SHEET 6 C 9 VAL C 179 ILE C 183 1 N ILE C 180 O LEU C 147
SHEET 7 C 9 LEU C 198 PRO C 202 1 N LEU C 198 O ILE C 180
SHEET 8 C 9 ILE C 230 VAL C 233 1 O ILE C 230 N THR C 201
SHEET 9 C 9 LEU C 32 SER C 35 1 N CYS C 33 O ILE C 231
SHEET 1 D 9 LEU D 32 SER D 35 0
SHEET 2 D 9 LEU D 57 THR D 60 1 O LEU D 57 N ALA D 34
SHEET 3 D 9 LEU D 87 PHE D 94 1 O LEU D 87 N LEU D 58
SHEET 4 D 9 ILE D 118 HIS D 122 1 N ILE D 118 O LEU D 88
SHEET 5 D 9 GLY D 146 LEU D 150 1 O GLY D 146 N THR D 119
SHEET 6 D 9 VAL D 179 ILE D 183 1 N ILE D 180 O LEU D 147
SHEET 7 D 9 LEU D 198 THR D 201 1 N LEU D 198 O ILE D 180
SHEET 8 D 9 ILE D 230 VAL D 233 1 O ILE D 230 N THR D 201
SHEET 9 D 9 LEU D 32 SER D 35 1 N CYS D 33 O ILE D 231
CRYST1 90.060 116.217 116.979 90.00 90.00 90.00 P 21 21 21 16
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 0.011104 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008605 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008549 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
