HEADER TRANSFERASE 21-NOV-07 3BFI
TITLE E. COLI THYMIDYLATE SYNTHASE Y209M MUTANT COMPLEXED WITH 5-NITRO-DUMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TS, TSASE;
COMPND 5 EC: 2.1.1.45;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: THYA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: XAC25 THY;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: BLUSCRIPT SK+
KEYWDS METHYLTRANSFERASE, NUCLEOTIDE BIOSYNTHESIS, REPRESSOR, RNA-BINDING,
KEYWDS 2 TRANSLATION REGULATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.A.ROBERTS,W.R.MONTFORT
REVDAT 6 30-AUG-23 3BFI 1 REMARK
REVDAT 5 20-OCT-21 3BFI 1 REMARK SEQADV LINK
REVDAT 4 18-APR-18 3BFI 1 REMARK
REVDAT 3 25-OCT-17 3BFI 1 REMARK
REVDAT 2 13-JUL-11 3BFI 1 VERSN
REVDAT 1 02-DEC-08 3BFI 0
JRNL AUTH W.B.ARENDALL,D.C.HYATT,S.A.ROBERTS,A.L.DAHLGRAN,F.MALEY,
JRNL AUTH 2 W.R.MONTFORT
JRNL TITL E.COLI THYMIDYLATE SYNTHASE COMPLEXED WITH 5-NITRO-2'-DEOXY
JRNL TITL 2 URIDINE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 17489
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 942
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1130
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2149
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 83
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.197
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.181
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.647
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2248 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3055 ; 1.657 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 264 ; 6.421 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 102 ;36.111 ;24.706
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 356 ;17.347 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;22.342 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 320 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1735 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 814 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1491 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 95 ; 0.133 ; 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): 48 ; 0.163 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.141 ; 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): 1362 ; 0.973 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2140 ; 1.711 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1025 ; 2.656 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 915 ; 4.217 ; 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 : 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 3BFI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045455.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-NOV-97
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.5
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 : ENRAF-NONIUS FR571
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : ENRAF-NONIUS FAST
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROCOR
REMARK 200 DATA SCALING SOFTWARE : PROCOR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18431
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 STARTING MODEL: 3TMS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M AMMONIUM SULFATE, 20 MM REMARK
REMARK 280 280 KH2PO4, 4 MM DTT, 4 MM 5-NO2-DUMP, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 66.51000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.51000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.51000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.51000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.51000
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 66.51000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 66.51000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 66.51000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 66.51000
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 66.51000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 66.51000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 66.51000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 66.51000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 66.51000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 66.51000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 66.51000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 66.51000
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 66.51000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 66.51000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 66.51000
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 66.51000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 66.51000
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 66.51000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 66.51000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 66.51000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 66.51000
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 66.51000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 66.51000
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
REMARK 350 TOTAL BURIED SURFACE AREA: 4810 ANGSTROM**2
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 66.51000
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 SG CYS A 146 C6 NDU A 266 2.14
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 CXM A 1 CA - C - N ANGL. DEV. = -13.2 DEGREES
REMARK 500 CXM A 1 O - C - N ANGL. DEV. = 11.7 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 TYR A 94 -75.33 -16.88
REMARK 500 ALA A 100 49.96 -159.08
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 SO4 A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDU A 266
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3B9H RELATED DB: PDB
REMARK 900 E.COLI THYMIDYLATE SYNTHASE COMPLEXED WITH 5-NITRO-2'-DEOXY URIDINE
DBREF 3BFI A 1 264 UNP P0A884 TYSY_ECOLI 1 264
SEQADV 3BFI MET A 209 UNP P0A884 TYR 209 ENGINEERED MUTATION
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 CYS 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 CYS HIS ALA PHE PHE GLN PHE TYR VAL ALA ASP
SEQRES 13 A 264 GLY LYS LEU SER CYS GLN LEU TYR GLN ARG SER CYS 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 CYS ASP LEU GLU
SEQRES 16 A 264 VAL GLY ASP PHE VAL TRP THR GLY GLY ASP THR HIS LEU
SEQRES 17 A 264 MET 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 3BFI CXM A 1 MET N-CARBOXYMETHIONINE
HET CXM A 1 11
HET SO4 A 265 5
HET NDU A 266 23
HETNAM CXM N-CARBOXYMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM NDU 2'-DEOXY-5-NITROURIDINE 5'-MONOPHOSPHATE
FORMUL 1 CXM C6 H11 N O4 S
FORMUL 2 SO4 O4 S 2-
FORMUL 3 NDU C9 H14 N3 O10 P
FORMUL 4 HOH *83(H2 O)
HELIX 1 1 CXM A 1 GLY A 15 1 15
HELIX 2 2 GLN A 39 GLY A 41 5 3
HELIX 3 3 HIS A 51 GLY A 65 1 15
HELIX 4 4 ILE A 69 ASN A 75 1 7
HELIX 5 5 VAL A 93 ALA A 100 1 8
HELIX 6 6 ASP A 110 ASP A 122 1 13
HELIX 7 7 ASN A 134 MET A 141 5 8
HELIX 8 8 GLY A 173 ASP A 193 1 21
HELIX 9 9 HIS A 212 LEU A 220 1 9
HELIX 10 10 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 O THR A 26 N LYS A 18
SHEET 3 A 6 GLU A 195 MET A 209 -1 O THR A 206 N ILE A 29
SHEET 4 A 6 LYS A 158 ASP A 169 1 N LEU A 159 O GLU A 195
SHEET 5 A 6 HIS A 147 ALA A 155 -1 N PHE A 149 O 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 O ILE A 109 N 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 O GLU A 248 N ILE A 231
LINK C CXM A 1 N LYS A 2 1555 1555 1.31
SITE 1 AC1 3 ARG A 49 PRO A 256 GLY A 257
SITE 1 AC2 19 ARG A 21 TRP A 80 TYR A 94 ARG A 126
SITE 2 AC2 19 ARG A 127 LEU A 143 CYS A 146 HIS A 147
SITE 3 AC2 19 GLN A 165 ARG A 166 SER A 167 CYS A 168
SITE 4 AC2 19 ASP A 169 ASN A 177 HIS A 207 MET A 209
SITE 5 AC2 19 HOH A 332 HOH A 334 HOH A 369
CRYST1 133.020 133.020 133.020 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 0.007518 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007518 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007518 0.00000
HETATM 1 N CXM A 1 -12.508 -1.044 15.757 1.00 29.56 N
HETATM 2 CA CXM A 1 -12.118 0.023 16.655 1.00 29.68 C
HETATM 3 CB CXM A 1 -13.357 0.707 17.248 1.00 30.33 C
HETATM 4 CG CXM A 1 -14.039 1.644 16.284 1.00 30.12 C
HETATM 5 SD CXM A 1 -15.606 2.314 16.878 1.00 33.52 S
HETATM 6 CE CXM A 1 -16.522 0.844 17.303 1.00 34.26 C
HETATM 7 C CXM A 1 -11.390 -0.696 17.765 1.00 29.85 C
HETATM 8 O CXM A 1 -11.756 -1.803 18.161 1.00 30.13 O
HETATM 9 CN CXM A 1 -12.516 -0.962 14.436 1.00 28.60 C
HETATM 10 ON1 CXM A 1 -12.453 0.134 13.875 1.00 28.60 O
HETATM 11 ON2 CXM A 1 -13.051 -1.895 13.833 1.00 31.28 O
(ATOM LINES ARE NOT SHOWN.)
END
