HEADER TRANSFERASE 19-APR-00 1EV8
TITLE CRYSTAL STRUCTURE ANALYSIS OF CYS167 MUTANT OF ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.1.1.45;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PBLUESCRIPT SK
KEYWDS CYS167 E. COLI THYMIDYLATE SYNTHASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PHAN,E.MAHDAVIAN,M.C.NIVENS,W.MINOR,S.BERGER,H.T.SPENCER,
AUTHOR 2 R.B.DUNLAP,L.LEBIODA
REVDAT 8 13-APR-22 1EV8 1 AUTHOR JRNL
REVDAT 7 03-NOV-21 1EV8 1 SEQADV LINK
REVDAT 6 31-JAN-18 1EV8 1 REMARK
REVDAT 5 04-OCT-17 1EV8 1 REMARK
REVDAT 4 13-JUL-11 1EV8 1 VERSN
REVDAT 3 24-FEB-09 1EV8 1 VERSN
REVDAT 2 29-NOV-00 1EV8 1 JRNL
REVDAT 1 03-MAY-00 1EV8 0
JRNL AUTH J.PHAN,E.MAHDAVIAN,M.C.NIVENS,W.MINOR,S.BERGER,H.T.SPENCER,
JRNL AUTH 2 R.B.DUNLAP,L.LEBIODA
JRNL TITL CATALYTIC CYSTEINE OF THYMIDYLATE SYNTHASE IS ACTIVATED UPON
JRNL TITL 2 SUBSTRATE BINDING.
JRNL REF BIOCHEMISTRY V. 39 6969 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10841779
JRNL DOI 10.1021/BI000367G
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2336470.490
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.4
REMARK 3 NUMBER OF REFLECTIONS : 9684
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) : 0.223
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 979
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.75
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 35.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 623
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 76
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2164
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 11
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.36
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.45
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.920
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 1.11
REMARK 3 BSOL : 137.4
REMARK 3
REMARK 3 NCS MODEL : NULL
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_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EV8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-98
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11099
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 6.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 12.27
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 31.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 68% SATURATED AMMONIUM SULFATE, 100 MM
REMARK 280 SODIUM PHOSPHATE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 18K, TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y,-Z
REMARK 290 16555 X,-Y,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z,-X,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y
REMARK 290 20555 -Z+1/2,X,-Y
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z,-X
REMARK 290 23555 Y,-Z,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X
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 68.13700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.13700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 68.13700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.13700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 68.13700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 68.13700
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 68.13700
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 68.13700
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 68.13700
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 68.13700
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 68.13700
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 68.13700
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 68.13700
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 68.13700
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 68.13700
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 68.13700
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 68.13700
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 68.13700
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 68.13700
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 68.13700
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 68.13700
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 68.13700
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 68.13700
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 68.13700
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 68.13700
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 68.13700
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 204.41100
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 LYS A 2 NZ
REMARK 470 GLU A 237 CG CD OE1 OE2
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 ASP A 20 N THR A 22 2.07
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 LYS A 18 -166.38 170.02
REMARK 500 ASP A 20 -152.37 -114.13
REMARK 500 ARG A 21 34.00 -48.87
REMARK 500 THR A 22 78.24 69.55
REMARK 500 PRO A 43 47.66 -77.85
REMARK 500 VAL A 93 -153.23 -75.35
REMARK 500 TYR A 94 -78.23 -40.90
REMARK 500 ALA A 100 55.49 -162.08
REMARK 500 ASP A 122 59.06 -152.45
REMARK 500 ARG A 127 41.63 -149.78
REMARK 500 ASN A 211 31.76 -86.95
REMARK 500 PRO A 228 -163.61 -77.34
REMARK 500 GLU A 245 3.55 -64.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EV5 RELATED DB: PDB
REMARK 900 S167A MUTANT OF E. COLI THYMIDYLATE SYNTHASE (MODIFIED CATALYTIC
REMARK 900 CYSTEINE)
REMARK 900 RELATED ID: 1EVF RELATED DB: PDB
REMARK 900 S167T MUTANT OF E. COLI THYMIDYLATE SYNTHASE (MODIFIED CATALYTIC
REMARK 900 CYSTEINE)
REMARK 900 RELATED ID: 1EVG RELATED DB: PDB
REMARK 900 S167T MUTANT OF E. COLI THYMIDYLATE SYNTHASE (UNMODIFIED CATALYTIC
REMARK 900 CYSTEINE)
DBREF 1EV8 A 1 264 UNP P0A884 TYSY_ECOLI 1 264
SEQADV 1EV8 CXM A 1 UNP P0A884 MET 1 MODIFIED RESIDUE
SEQADV 1EV8 CME A 50 UNP P0A884 CYS 50 MODIFIED RESIDUE
SEQADV 1EV8 CME A 146 UNP P0A884 CYS 146 MODIFIED RESIDUE
SEQADV 1EV8 CYS A 167 UNP P0A884 SER 167 ENGINEERED MUTATION
SEQADV 1EV8 CME A 168 UNP P0A884 CYS 168 MODIFIED RESIDUE
SEQADV 1EV8 CME A 192 UNP P0A884 CYS 192 MODIFIED RESIDUE
SEQRES 1 A 264 CXM LYS GLN TYR LEU GLU LEU MET GLN LYS VAL LEU ASP
SEQRES 2 A 264 GLU GLY THR GLN LYS ASN ASP ARG THR GLY THR GLY THR
SEQRES 3 A 264 LEU SER ILE PHE GLY HIS GLN MET ARG PHE ASN LEU GLN
SEQRES 4 A 264 ASP GLY PHE PRO LEU VAL THR THR LYS ARG CME HIS LEU
SEQRES 5 A 264 ARG SER ILE ILE HIS GLU LEU LEU TRP PHE LEU GLN GLY
SEQRES 6 A 264 ASP THR ASN ILE ALA TYR LEU HIS GLU ASN ASN VAL THR
SEQRES 7 A 264 ILE TRP ASP GLU TRP ALA ASP GLU ASN GLY ASP LEU GLY
SEQRES 8 A 264 PRO VAL TYR GLY LYS GLN TRP ARG ALA TRP PRO THR PRO
SEQRES 9 A 264 ASP GLY ARG HIS ILE ASP GLN ILE THR THR VAL LEU ASN
SEQRES 10 A 264 GLN LEU LYS ASN ASP PRO ASP SER ARG ARG ILE ILE VAL
SEQRES 11 A 264 SER ALA TRP ASN VAL GLY GLU LEU ASP LYS MET ALA LEU
SEQRES 12 A 264 ALA PRO CME HIS ALA PHE PHE GLN PHE TYR VAL ALA ASP
SEQRES 13 A 264 GLY LYS LEU SER CYS GLN LEU TYR GLN ARG CYS CME ASP
SEQRES 14 A 264 VAL PHE LEU GLY LEU PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 15 A 264 LEU LEU VAL HIS MET MET ALA GLN GLN CME ASP LEU GLU
SEQRES 16 A 264 VAL GLY ASP PHE VAL TRP THR GLY GLY ASP THR HIS LEU
SEQRES 17 A 264 TYR SER ASN HIS MET ASP GLN THR HIS LEU GLN LEU SER
SEQRES 18 A 264 ARG GLU PRO ARG PRO LEU PRO LYS LEU ILE ILE LYS ARG
SEQRES 19 A 264 LYS PRO GLU SER ILE PHE ASP TYR ARG PHE GLU ASP PHE
SEQRES 20 A 264 GLU ILE GLU GLY TYR ASP PRO HIS PRO GLY ILE LYS ALA
SEQRES 21 A 264 PRO VAL ALA ILE
MODRES 1EV8 CXM A 1 MET N-CARBOXYMETHIONINE
MODRES 1EV8 CME A 50 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1EV8 CME A 146 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1EV8 CME A 168 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1EV8 CME A 192 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CXM A 1 11
HET CME A 50 10
HET CME A 146 10
HET CME A 168 10
HET CME A 192 10
HETNAM CXM N-CARBOXYMETHIONINE
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
FORMUL 1 CXM C6 H11 N O4 S
FORMUL 1 CME 4(C5 H11 N O3 S2)
FORMUL 2 HOH *11(H2 O)
HELIX 1 1 LYS A 2 GLY A 15 1 14
HELIX 2 2 GLN A 39 GLY A 41 5 3
HELIX 3 3 LEU A 52 GLN A 64 1 13
HELIX 4 4 ILE A 69 ASN A 75 1 7
HELIX 5 5 TRP A 80 ALA A 84 5 5
HELIX 6 6 VAL A 93 ALA A 100 1 8
HELIX 7 7 ASP A 110 ASP A 122 1 13
HELIX 8 8 ASN A 134 MET A 141 5 8
HELIX 9 9 GLY A 173 GLN A 191 1 19
HELIX 10 10 HIS A 212 LEU A 220 1 9
HELIX 11 11 ARG A 243 GLU A 245 5 3
SHEET 1 A 6 THR A 16 ASN A 19 0
SHEET 2 A 6 GLY A 25 ASN A 37 -1 N THR A 26 O LYS A 18
SHEET 3 A 6 GLU A 195 TYR A 209 -1 O PHE A 199 N PHE A 36
SHEET 4 A 6 LYS A 158 GLN A 165 1 O LEU A 159 N GLY A 197
SHEET 5 A 6 PHE A 149 ALA A 155 -1 O PHE A 149 N TYR A 164
SHEET 6 A 6 ILE A 129 SER A 131 -1 N VAL A 130 O PHE A 150
SHEET 1 B 2 TRP A 101 PRO A 102 0
SHEET 2 B 2 HIS A 108 ILE A 109 -1 N ILE A 109 O TRP A 101
SHEET 1 C 2 LYS A 229 ILE A 232 0
SHEET 2 C 2 PHE A 247 GLU A 250 -1 N GLU A 248 O ILE A 231
LINK C CXM A 1 N LYS A 2 1555 1555 1.35
LINK C ARG A 49 N CME A 50 1555 1555 1.33
LINK C CME A 50 N HIS A 51 1555 1555 1.33
LINK C PRO A 145 N CME A 146 1555 1555 1.32
LINK C CME A 146 N HIS A 147 1555 1555 1.33
LINK C CYS A 167 N CME A 168 1555 1555 1.34
LINK C CME A 168 N ASP A 169 1555 1555 1.32
LINK C GLN A 191 N CME A 192 1555 1555 1.33
LINK C CME A 192 N ASP A 193 1555 1555 1.33
CRYST1 136.274 136.274 136.274 90.00 90.00 90.00 I 21 3 24
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 0.007338 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007338 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007338 0.00000
HETATM 1 N CXM A 1 21.531 18.044 101.092 1.00 27.32 N
HETATM 2 CA CXM A 1 21.851 17.076 102.254 1.00 28.16 C
HETATM 3 CB CXM A 1 20.560 16.542 102.944 1.00 28.17 C
HETATM 4 CG CXM A 1 19.644 17.624 103.519 1.00 28.59 C
HETATM 5 SD CXM A 1 18.101 17.072 104.306 1.00 30.31 S
HETATM 6 CE CXM A 1 17.083 16.485 102.844 1.00 26.74 C
HETATM 7 C CXM A 1 22.649 15.829 101.813 1.00 28.32 C
HETATM 8 O CXM A 1 22.347 15.238 100.758 1.00 27.43 O
HETATM 9 CN CXM A 1 21.372 19.365 101.356 1.00 27.62 C
HETATM 10 ON1 CXM A 1 21.188 20.165 100.410 1.00 27.54 O
HETATM 11 ON2 CXM A 1 21.482 19.820 102.531 1.00 26.25 O
(ATOM LINES ARE NOT SHOWN.)
END
