HEADER TRANSFERASE 09-OCT-14 4WML
TITLE CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE OMP SYNTHASE IN COMPLEX
TITLE 2 WITH PRP(CH2)P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OROTATE PHOSPHORIBOSYLTRANSFERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OPRTASE 1;
COMPND 5 EC: 2.4.2.10;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: URA5, PYR5, YML106W, YM8339.13;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.B.BANG,U.MOLICH,M.R.HANSEN,C.GRUBMEYER,P.HARRIS
REVDAT 4 10-JAN-24 4WML 1 HETSYN
REVDAT 3 29-JUL-20 4WML 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 17-JAN-18 4WML 1 REMARK
REVDAT 1 23-DEC-15 4WML 0
JRNL AUTH M.B.BANG,U.MOLICH,M.R.HANSEN,C.GRUBMEYER,P.HARRIS
JRNL TITL CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIA OMP SYNTHASE IN
JRNL TITL 2 COMPLEX WITH PRP(CH2)P
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 25402
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1337
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) : 1.73
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.78
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1886
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3300
REMARK 3 BIN FREE R VALUE SET COUNT : 100
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1668
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.68000
REMARK 3 B22 (A**2) : 1.68000
REMARK 3 B33 (A**2) : -3.35000
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): 0.120
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.112
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.707
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1738 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1724 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2351 ; 1.984 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3969 ; 0.936 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 220 ; 6.169 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 71 ;31.303 ;24.789
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 319 ;15.734 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;14.946 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 276 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1931 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 379 ; 0.001 ; 0.020
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): 871 ; 3.586 ; 3.511
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 870 ; 3.583 ; 3.506
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1088 ; 5.134 ; 5.246
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1089 ; 5.132 ; 5.252
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 867 ; 4.275 ; 3.938
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 863 ; 4.250 ; 3.940
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1256 ; 6.401 ; 5.695
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2074 ; 8.040 ;28.521
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2031 ; 8.013 ;28.308
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 : NULL
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4WML COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000204086.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26807
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730
REMARK 200 RESOLUTION RANGE LOW (A) : 33.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.6300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.450
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2PRY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAHEPES PH 7.5, 10 %
REMARK 280 ISOPROPANOL, 20 % PEG 4000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 66.24500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.78000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.78000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 99.36750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.78000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.78000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.12250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.78000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.78000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 99.36750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.78000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.78000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 33.12250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 66.24500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 438 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 449 LIES ON A SPECIAL POSITION.
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 PRO A 1
REMARK 465 ALA A 108
REMARK 465 LYS A 109
REMARK 465 ASP A 110
REMARK 465 HIS A 111
REMARK 465 GLY A 112
REMARK 465 GLU A 113
REMARK 465 GLY A 114
REMARK 465 ALA A 225
REMARK 465 GLU A 226
REMARK 465 ASN A 227
REMARK 465 LEU A 228
REMARK 465 TYR A 229
REMARK 465 PHE A 230
REMARK 465 GLN A 231
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 O TYR A 201 NH1 ARG A 205 2.10
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 135 -86.54 -125.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PPC A 302 O1
REMARK 620 2 PPC A 302 O2B 86.3
REMARK 620 3 PPC A 302 O2 71.9 95.9
REMARK 620 4 PPC A 302 O3 83.6 167.6 74.1
REMARK 620 5 HOH A 456 O 164.0 96.8 92.2 91.1
REMARK 620 6 HOH A 457 O 101.7 91.9 169.4 97.1 93.9
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PRY RELATED DB: PDB
REMARK 900 2PRY CONTAINS THE SAME PROTEIN IN APO FORM
REMARK 900 RELATED ID: 2PRZ RELATED DB: PDB
REMARK 900 2PRZ CONTAINS THE SAME PROTEIN COMPLEXED WITH OMP
REMARK 900 RELATED ID: 2PS1 RELATED DB: PDB
REMARK 900 2PS1 CONTAINS THE SAME PROTEIN COMPLEXED WITH OROTATE, MG2+ AND PRPP
DBREF 4WML A 1 225 UNP P13298 PYRE_YEAST 2 226
SEQADV 4WML GLU A 226 UNP P13298 EXPRESSION TAG
SEQADV 4WML ASN A 227 UNP P13298 EXPRESSION TAG
SEQADV 4WML LEU A 228 UNP P13298 EXPRESSION TAG
SEQADV 4WML TYR A 229 UNP P13298 EXPRESSION TAG
SEQADV 4WML PHE A 230 UNP P13298 EXPRESSION TAG
SEQADV 4WML GLN A 231 UNP P13298 EXPRESSION TAG
SEQRES 1 A 231 PRO ILE MET LEU GLU ASP TYR GLN LYS ASN PHE LEU GLU
SEQRES 2 A 231 LEU ALA ILE GLU CYS GLN ALA LEU ARG PHE GLY SER PHE
SEQRES 3 A 231 LYS LEU LYS SER GLY ARG GLU SER PRO TYR PHE PHE ASN
SEQRES 4 A 231 LEU GLY LEU PHE ASN THR GLY LYS LEU LEU SER ASN LEU
SEQRES 5 A 231 ALA THR ALA TYR ALA ILE ALA ILE ILE GLN SER ASP LEU
SEQRES 6 A 231 LYS PHE ASP VAL ILE PHE GLY PRO ALA TYR LYS GLY ILE
SEQRES 7 A 231 PRO LEU ALA ALA ILE VAL CYS VAL LYS LEU ALA GLU ILE
SEQRES 8 A 231 GLY GLY SER LYS PHE GLN ASN ILE GLN TYR ALA PHE ASN
SEQRES 9 A 231 ARG LYS GLU ALA LYS ASP HIS GLY GLU GLY GLY ILE ILE
SEQRES 10 A 231 VAL GLY SER ALA LEU GLU ASN LYS ARG ILE LEU ILE ILE
SEQRES 11 A 231 ASP ASP VAL MET THR ALA GLY THR ALA ILE ASN GLU ALA
SEQRES 12 A 231 PHE GLU ILE ILE SER ASN ALA LYS GLY GLN VAL VAL GLY
SEQRES 13 A 231 SER ILE ILE ALA LEU ASP ARG GLN GLU VAL VAL SER THR
SEQRES 14 A 231 ASP ASP LYS GLU GLY LEU SER ALA THR GLN THR VAL SER
SEQRES 15 A 231 LYS LYS TYR GLY ILE PRO VAL LEU SER ILE VAL SER LEU
SEQRES 16 A 231 ILE HIS ILE ILE THR TYR LEU GLU GLY ARG ILE THR ALA
SEQRES 17 A 231 GLU GLU LYS SER LYS ILE GLU GLN TYR LEU GLN THR TYR
SEQRES 18 A 231 GLY ALA SER ALA GLU ASN LEU TYR PHE GLN
HET MG A 301 1
HET PPC A 302 22
HETNAM MG MAGNESIUM ION
HETNAM PPC 1-O-[(R)-HYDROXY(PHOSPHONOMETHYL)PHOSPHORYL]-5-O-
HETNAM 2 PPC PHOSPHONO-ALPHA-D-RIBOFURANOSE
HETSYN PPC 5-PHOSPHORIBOSYL-1-(BETA-METHYLENE) PYROPHOSPHATE; 1-O-
HETSYN 2 PPC [(R)-HYDROXY(PHOSPHONOMETHYL)PHOSPHORYL]-5-O-
HETSYN 3 PPC PHOSPHONO-ALPHA-D-RIBOSE; 1-O-[(R)-
HETSYN 4 PPC HYDROXY(PHOSPHONOMETHYL)PHOSPHORYL]-5-O-PHOSPHONO-D-
HETSYN 5 PPC RIBOSE; 1-O-[(R)-HYDROXY(PHOSPHONOMETHYL)PHOSPHORYL]-
HETSYN 6 PPC 5-O-PHOSPHONO-RIBOSE
FORMUL 2 MG MG 2+
FORMUL 3 PPC C6 H15 O13 P3
FORMUL 4 HOH *139(H2 O)
HELIX 1 AA1 GLU A 5 CYS A 18 1 14
HELIX 2 AA2 LEU A 40 PHE A 43 5 4
HELIX 3 AA3 THR A 45 SER A 63 1 19
HELIX 4 AA4 LYS A 76 GLY A 92 1 17
HELIX 5 AA5 GLY A 93 GLN A 97 5 5
HELIX 6 AA6 GLY A 137 ALA A 150 1 14
HELIX 7 AA7 SER A 176 GLY A 186 1 11
HELIX 8 AA8 LEU A 195 GLU A 203 1 9
HELIX 9 AA9 THR A 207 GLY A 222 1 16
SHEET 1 AA1 2 LEU A 21 LYS A 27 0
SHEET 2 AA1 2 GLU A 33 PHE A 38 -1 O SER A 34 N PHE A 26
SHEET 1 AA2 6 ILE A 117 VAL A 118 0
SHEET 2 AA2 6 GLN A 100 ASN A 104 -1 N PHE A 103 O VAL A 118
SHEET 3 AA2 6 VAL A 69 GLY A 72 1 N ILE A 70 O GLN A 100
SHEET 4 AA2 6 ARG A 126 ILE A 130 1 O LEU A 128 N PHE A 71
SHEET 5 AA2 6 GLN A 153 ASP A 162 1 O VAL A 155 N ILE A 127
SHEET 6 AA2 6 VAL A 189 SER A 194 1 O LEU A 190 N SER A 157
LINK MG MG A 301 O1 PPC A 302 1555 1555 2.32
LINK MG MG A 301 O2B PPC A 302 1555 1555 1.91
LINK MG MG A 301 O2 PPC A 302 1555 1555 2.10
LINK MG MG A 301 O3 PPC A 302 1555 1555 2.24
LINK MG MG A 301 O HOH A 456 1555 1555 2.02
LINK MG MG A 301 O HOH A 457 1555 1555 2.14
CISPEP 1 ALA A 74 TYR A 75 0 -4.70
CRYST1 61.560 61.560 132.490 90.00 90.00 90.00 P 43 21 2 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 0.016244 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016244 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007548 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
