HEADER TRANSFERASE 20-AUG-98 1BQ1
TITLE E. COLI THYMIDYLATE SYNTHASE MUTANT N177A IN COMPLEX WITH CB3717 AND
TITLE 2 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (DUMP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A, B;
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 CELL_LINE: X2913;
SOURCE 5 GENE: THYA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: BLUESCRIPT VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTHYA-N177A;
SOURCE 10 EXPRESSION_SYSTEM_GENE: THYA
KEYWDS TRANSFERASE, ACTIVE SITE MUTANT, REACTION INTERMEDIATE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.L.REYES,C.R.SAGE,E.E.RUTENBER,J.S.FINER-MOORE,R.M.STROUD
REVDAT 6 03-NOV-21 1BQ1 1 REMARK SEQADV LINK
REVDAT 5 11-APR-18 1BQ1 1 REMARK
REVDAT 4 04-APR-18 1BQ1 1 REMARK
REVDAT 3 13-JUL-11 1BQ1 1 VERSN
REVDAT 2 24-FEB-09 1BQ1 1 VERSN
REVDAT 1 18-MAY-99 1BQ1 0
JRNL AUTH C.L.REYES,C.R.SAGE,E.E.RUTENBER,R.M.NISSEN,J.S.FINER-MOORE,
JRNL AUTH 2 R.M.STROUD
JRNL TITL INACTIVITY OF N229A THYMIDYLATE SYNTHASE DUE TO
JRNL TITL 2 WATER-MEDIATED EFFECTS: ISOLATING A LATE STAGE IN METHYL
JRNL TITL 3 TRANSFER.
JRNL REF J.MOL.BIOL. V. 284 699 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9826509
JRNL DOI 10.1006/JMBI.1998.2205
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.3
REMARK 3 NUMBER OF REFLECTIONS : 20033
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) : 0.152
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1993
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.65
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2820
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 323
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4300
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 110
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.90
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.21
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) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 2.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.370
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.970 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.410 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.570 ; 1.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.200 ; 2.000
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 : SAGEE58Q_PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : SAGEE58Q_PARAM11.WAT
REMARK 3 PARAMETER FILE 3 : SAGEE58Q_PARAMED.LIG
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : SAGEE58Q_TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : SAGEE58Q_TOPH11.WAT
REMARK 3 TOPOLOGY FILE 3 : SAGEE58Q_TOPO_COV.DUMP
REMARK 3 TOPOLOGY FILE 4 : SAGEE58Q_TOPO.CB3
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BQ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171995.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JAN-95
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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 R-AXIS II
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 II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23346
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.7
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
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 34.08900
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 34.08900
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 34.08900
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: 8030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 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 HZ3 LYS A 10 HD1 HIS A 32 1.26
REMARK 500 HZ3 LYS B 10 HD1 HIS B 32 1.28
REMARK 500 HZ3 LYS A 48 H2 HOH A 677 1.34
REMARK 500 O SER A 125 H1 HOH A 835 1.57
REMARK 500
REMARK 500 REMARK: NULL
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 HIS A 51 NE2 HIS A 51 CD2 -0.068
REMARK 500 HIS A 73 NE2 HIS A 73 CD2 -0.078
REMARK 500 HIS A 108 NE2 HIS A 108 CD2 -0.068
REMARK 500 HIS A 147 NE2 HIS A 147 CD2 -0.081
REMARK 500 HIS A 207 NE2 HIS A 207 CD2 -0.067
REMARK 500 HIS A 212 NE2 HIS A 212 CD2 -0.070
REMARK 500 HIS A 217 NE2 HIS A 217 CD2 -0.075
REMARK 500 HIS A 255 NE2 HIS A 255 CD2 -0.070
REMARK 500 HIS B 51 NE2 HIS B 51 CD2 -0.068
REMARK 500 HIS B 57 NE2 HIS B 57 CD2 -0.072
REMARK 500 HIS B 73 NE2 HIS B 73 CD2 -0.069
REMARK 500 HIS B 108 NE2 HIS B 108 CD2 -0.069
REMARK 500 HIS B 147 NE2 HIS B 147 CD2 -0.070
REMARK 500 HIS B 186 NE2 HIS B 186 CD2 -0.070
REMARK 500 HIS B 207 NE2 HIS B 207 CD2 -0.070
REMARK 500 HIS B 212 NE2 HIS B 212 CD2 -0.070
REMARK 500 HIS B 217 NE2 HIS B 217 CD2 -0.069
REMARK 500 HIS B 255 NE2 HIS B 255 CD2 -0.067
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 ARG A 53 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TRP A 61 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 61 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 80 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP A 80 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 83 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 83 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP A 98 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP A 98 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 TRP A 101 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 101 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 133 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 133 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP A 201 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP A 201 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 TYR A 252 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 35 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 35 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 TRP B 61 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP B 61 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 TRP B 80 CD1 - CG - CD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 TRP B 80 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP B 80 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP B 83 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP B 83 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TRP B 98 CD1 - CG - CD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 TRP B 98 CE2 - CD2 - CG ANGL. DEV. = -5.1 DEGREES
REMARK 500 TRP B 101 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP B 101 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG B 126 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TRP B 133 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP B 133 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP B 201 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP B 201 CE2 - CD2 - CG ANGL. DEV. = -5.8 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 PRO A 92 57.01 -67.26
REMARK 500 VAL A 93 -158.63 -80.08
REMARK 500 TYR A 94 -70.17 -30.19
REMARK 500 ALA A 100 55.55 -158.93
REMARK 500 ASP A 122 50.23 -145.94
REMARK 500 ASP B 81 -39.97 -39.50
REMARK 500 ASP B 85 -177.18 -67.77
REMARK 500 TYR B 94 -54.07 -27.81
REMARK 500 ALA B 100 62.45 -159.32
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 UMP A 565
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CB3 A 566
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP B 567
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CB3 B 568
DBREF 1BQ1 A 2 264 UNP P0A884 TYSY_ECOLI 2 264
DBREF 1BQ1 B 2 264 UNP P0A884 TYSY_ECOLI 2 264
SEQADV 1BQ1 ALA A 177 UNP P0A884 ASN 177 ENGINEERED MUTATION
SEQADV 1BQ1 ALA B 177 UNP P0A884 ASN 177 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 ALA 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 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
SEQRES 1 B 264 CXM LYS GLN TYR LEU GLU LEU MET GLN LYS VAL LEU ASP
SEQRES 2 B 264 GLU GLY THR GLN LYS ASN ASP ARG THR GLY THR GLY THR
SEQRES 3 B 264 LEU SER ILE PHE GLY HIS GLN MET ARG PHE ASN LEU GLN
SEQRES 4 B 264 ASP GLY PHE PRO LEU VAL THR THR LYS ARG CYS HIS LEU
SEQRES 5 B 264 ARG SER ILE ILE HIS GLU LEU LEU TRP PHE LEU GLN GLY
SEQRES 6 B 264 ASP THR ASN ILE ALA TYR LEU HIS GLU ASN ASN VAL THR
SEQRES 7 B 264 ILE TRP ASP GLU TRP ALA ASP GLU ASN GLY ASP LEU GLY
SEQRES 8 B 264 PRO VAL TYR GLY LYS GLN TRP ARG ALA TRP PRO THR PRO
SEQRES 9 B 264 ASP GLY ARG HIS ILE ASP GLN ILE THR THR VAL LEU ASN
SEQRES 10 B 264 GLN LEU LYS ASN ASP PRO ASP SER ARG ARG ILE ILE VAL
SEQRES 11 B 264 SER ALA TRP ASN VAL GLY GLU LEU ASP LYS MET ALA LEU
SEQRES 12 B 264 ALA PRO CYS HIS ALA PHE PHE GLN PHE TYR VAL ALA ASP
SEQRES 13 B 264 GLY LYS LEU SER CYS GLN LEU TYR GLN ARG SER CYS ASP
SEQRES 14 B 264 VAL PHE LEU GLY LEU PRO PHE ALA ILE ALA SER TYR ALA
SEQRES 15 B 264 LEU LEU VAL HIS MET MET ALA GLN GLN CYS ASP LEU GLU
SEQRES 16 B 264 VAL GLY ASP PHE VAL TRP THR GLY GLY ASP THR HIS LEU
SEQRES 17 B 264 TYR SER ASN HIS MET ASP GLN THR HIS LEU GLN LEU SER
SEQRES 18 B 264 ARG GLU PRO ARG PRO LEU PRO LYS LEU ILE ILE LYS ARG
SEQRES 19 B 264 LYS PRO GLU SER ILE PHE ASP TYR ARG PHE GLU ASP PHE
SEQRES 20 B 264 GLU ILE GLU GLY TYR ASP PRO HIS PRO GLY ILE LYS ALA
SEQRES 21 B 264 PRO VAL ALA ILE
MODRES 1BQ1 CXM A 1 MET N-CARBOXYMETHIONINE
MODRES 1BQ1 CXM B 1 MET N-CARBOXYMETHIONINE
HET CXM A 1 12
HET CXM B 1 12
HET UMP A 565 21
HET CB3 A 566 39
HET UMP B 567 21
HET CB3 B 568 39
HETNAM CXM N-CARBOXYMETHIONINE
HETNAM UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE
HETNAM CB3 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID
HETSYN UMP DUMP
FORMUL 1 CXM 2(C6 H11 N O4 S)
FORMUL 3 UMP 2(C9 H13 N2 O8 P)
FORMUL 4 CB3 2(C24 H23 N5 O6)
FORMUL 7 HOH *228(H2 O)
HELIX 1 1 LYS A 2 GLU A 14 1 13
HELIX 2 2 LEU A 38 ASP A 40 5 3
HELIX 3 3 LEU A 52 GLN A 64 1 13
HELIX 4 4 ILE A 69 ASN A 75 5 7
HELIX 5 5 ASP A 81 TRP A 83 5 3
HELIX 6 6 TYR A 94 ALA A 100 1 7
HELIX 7 7 GLN A 111 ASN A 121 1 11
HELIX 8 8 VAL A 135 LYS A 140 5 6
HELIX 9 9 GLY A 173 GLN A 191 1 19
HELIX 10 10 SER A 210 SER A 221 5 12
HELIX 11 11 ILE A 239 ASP A 241 5 3
HELIX 12 12 PHE A 244 ASP A 246 5 3
HELIX 13 13 LYS B 2 GLU B 14 1 13
HELIX 14 14 LEU B 52 LEU B 63 1 12
HELIX 15 15 ALA B 70 ASN B 75 1 6
HELIX 16 16 TYR B 94 ALA B 100 1 7
HELIX 17 17 GLN B 111 ASN B 121 1 11
HELIX 18 18 VAL B 135 LYS B 140 5 6
HELIX 19 19 GLY B 173 GLN B 191 1 19
HELIX 20 20 SER B 210 SER B 221 5 12
HELIX 21 21 ILE B 239 ASP B 241 5 3
HELIX 22 22 PHE B 244 ASP B 246 5 3
SHEET 1 A 4 THR A 16 LYS A 18 0
SHEET 2 A 4 THR A 26 PHE A 30 -1 N SER A 28 O THR A 16
SHEET 3 A 4 ASP A 205 TYR A 209 -1 N LEU A 208 O LEU A 27
SHEET 4 A 4 SER A 167 ASP A 169 1 N CYS A 168 O ASP A 205
SHEET 1 B 5 HIS A 32 ASN A 37 0
SHEET 2 B 5 ASP A 198 GLY A 203 -1 N GLY A 203 O HIS A 32
SHEET 3 B 5 LYS A 158 GLN A 165 1 N CYS A 161 O VAL A 200
SHEET 4 B 5 HIS A 147 ALA A 155 -1 N ALA A 155 O LYS A 158
SHEET 5 B 5 ILE A 129 SER A 131 -1 N VAL A 130 O PHE A 150
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 250 O LYS A 229
SHEET 1 D 4 THR B 16 LYS B 18 0
SHEET 2 D 4 THR B 26 PHE B 30 -1 N SER B 28 O THR B 16
SHEET 3 D 4 ASP B 205 TYR B 209 -1 N LEU B 208 O LEU B 27
SHEET 4 D 4 SER B 167 ASP B 169 1 N CYS B 168 O ASP B 205
SHEET 1 E 5 HIS B 32 ASN B 37 0
SHEET 2 E 5 ASP B 198 GLY B 203 -1 N GLY B 203 O HIS B 32
SHEET 3 E 5 LYS B 158 GLN B 165 1 N CYS B 161 O VAL B 200
SHEET 4 E 5 HIS B 147 ALA B 155 -1 N ALA B 155 O LYS B 158
SHEET 5 E 5 ILE B 129 SER B 131 -1 N VAL B 130 O PHE B 150
SHEET 1 F 2 LYS B 229 ILE B 232 0
SHEET 2 F 2 PHE B 247 GLU B 250 -1 N GLU B 250 O LYS B 229
LINK C CXM A 1 N LYS A 2 1555 1555 1.33
LINK SG CYS A 146 C6 UMP A 565 1555 1555 1.82
LINK C CXM B 1 N LYS B 2 1555 1555 1.33
LINK SG CYS B 146 C6 UMP B 567 1555 1555 1.84
SITE 1 AC1 16 ARG A 21 CYS A 146 HIS A 147 GLN A 165
SITE 2 AC1 16 ARG A 166 SER A 167 CYS A 168 ASP A 169
SITE 3 AC1 16 HIS A 207 TYR A 209 CB3 A 566 HOH A 653
SITE 4 AC1 16 HOH A 708 HOH A 911 ARG B 126 ARG B 127
SITE 1 AC2 14 HIS A 51 SER A 54 ILE A 79 TRP A 83
SITE 2 AC2 14 ASP A 169 LEU A 172 GLY A 173 PHE A 176
SITE 3 AC2 14 LYS A 259 ALA A 263 UMP A 565 HOH A 677
SITE 4 AC2 14 HOH A 685 HOH A 901
SITE 1 AC3 14 ARG A 126 ARG A 127 ARG B 21 CYS B 146
SITE 2 AC3 14 HIS B 147 GLN B 165 ARG B 166 SER B 167
SITE 3 AC3 14 CYS B 168 ASP B 169 HIS B 207 TYR B 209
SITE 4 AC3 14 CB3 B 568 HOH B 785
SITE 1 AC4 15 HIS B 51 ILE B 79 TRP B 83 ASP B 169
SITE 2 AC4 15 LEU B 172 GLY B 173 PHE B 176 TYR B 209
SITE 3 AC4 15 VAL B 262 ALA B 263 UMP B 567 HOH B 801
SITE 4 AC4 15 HOH B 802 HOH B 821 HOH B 902
CRYST1 127.221 127.221 68.178 90.00 90.00 120.00 P 63 12
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 0.007860 0.004538 0.000000 0.00000
SCALE2 0.000000 0.009076 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014667 0.00000
MTRIX1 1 -0.999813 -0.018790 0.004533 61.82514 1
MTRIX2 1 0.015378 -0.631165 0.775496 22.17302 1
MTRIX3 1 -0.011710 0.775421 0.631336 -10.64110 1
HETATM 1 N CXM A 1 22.243 20.348 49.576 1.00 13.41 N
HETATM 2 CA CXM A 1 23.637 20.762 49.762 1.00 13.47 C
HETATM 3 CB CXM A 1 24.529 20.446 48.564 1.00 12.48 C
HETATM 4 CG CXM A 1 24.893 18.987 48.356 1.00 17.17 C
HETATM 5 SD CXM A 1 25.928 18.806 46.882 1.00 12.16 S
HETATM 6 CE CXM A 1 24.689 18.968 45.629 1.00 12.50 C
HETATM 7 C CXM A 1 23.619 22.267 49.892 1.00 9.99 C
HETATM 8 O CXM A 1 22.894 22.929 49.135 1.00 13.90 O
HETATM 9 CN CXM A 1 21.729 19.262 50.119 1.00 14.99 C
HETATM 10 ON1 CXM A 1 20.653 19.044 49.591 1.00 13.94 O
HETATM 11 ON2 CXM A 1 22.360 18.363 50.643 1.00 19.85 O
HETATM 12 H1 CXM A 1 21.643 20.924 49.055 1.00 15.00 H
(ATOM LINES ARE NOT SHOWN.)
END
