HEADER TRANSFERASE 21-SEP-07 2RD8
TITLE HUMAN THYMIDYLATE SYNTHASE STABILIZED IN ACTIVE CONFORMATION BY R163K
TITLE 2 MUTATION: ASYMMETRY AND REACTIVITY OF CYS195
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;
COMPND 8 OTHER_DETAILS: CYS AT POSITION 195;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 11 CHAIN: B;
COMPND 12 EC: 2.1.1.45;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES;
COMPND 15 OTHER_DETAILS: CME AT POSITION 195
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: TYMS, TS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 GENE: TYMS, TS;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS METHYL TRANSFERASE, METHYLTRANSFERASE, NUCLEOTIDE BIOSYNTHESIS,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.GIBSON,L.L.LOVELACE,L.LEBIODA
REVDAT 5 30-AUG-23 2RD8 1 REMARK
REVDAT 4 20-OCT-21 2RD8 1 REMARK SEQADV LINK
REVDAT 3 25-OCT-17 2RD8 1 REMARK
REVDAT 2 24-FEB-09 2RD8 1 VERSN
REVDAT 1 27-MAY-08 2RD8 0
JRNL AUTH L.M.GIBSON,L.L.LOVELACE,L.LEBIODA
JRNL TITL THE R163K MUTANT OF HUMAN THYMIDYLATE SYNTHASE IS STABILIZED
JRNL TITL 2 IN AN ACTIVE CONFORMATION: STRUCTURAL ASYMMETRY AND
JRNL TITL 3 REACTIVITY OF CYSTEINE 195.
JRNL REF BIOCHEMISTRY V. 47 4636 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18370400
JRNL DOI 10.1021/BI7019386
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 70.4
REMARK 3 NUMBER OF REFLECTIONS : 26954
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) : 0.228
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2711
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4566
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.35600
REMARK 3 B22 (A**2) : -10.35600
REMARK 3 B33 (A**2) : 20.71200
REMARK 3 B12 (A**2) : -13.84600
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.330
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.774 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.977 ; 2.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.248 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.869 ; 3.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 25.19
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.PARAMHICUP
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : BME.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOPHICUP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : BME.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2RD8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000044719.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97243
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 : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30034
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 33.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 69.6
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.13800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
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) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 15.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.46500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.800
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: 1HVY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20% PEG 4000, 3MM POTASSIUM
REMARK 280 PHOSPHATE, 20MM 2-MERCAPTOETHANOL, 0.1M TRIS, PH 9.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 86.51400
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 43.25700
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 43.25700
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 86.51400
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: 5070 ANGSTROM**2
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 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 MET A 1
REMARK 465 PRO A 2
REMARK 465 VAL A 3
REMARK 465 ALA A 4
REMARK 465 GLY A 5
REMARK 465 SER A 6
REMARK 465 GLU A 7
REMARK 465 LEU A 8
REMARK 465 PRO A 9
REMARK 465 ARG A 10
REMARK 465 ARG A 11
REMARK 465 PRO A 12
REMARK 465 LEU A 13
REMARK 465 PRO A 14
REMARK 465 PRO A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 GLN A 18
REMARK 465 GLU A 19
REMARK 465 ARG A 20
REMARK 465 ASP A 21
REMARK 465 ALA A 22
REMARK 465 GLU A 23
REMARK 465 PRO A 24
REMARK 465 ARG A 25
REMARK 465 MET A 309
REMARK 465 GLU A 310
REMARK 465 MET A 311
REMARK 465 ALA A 312
REMARK 465 VAL A 313
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 VAL B 3
REMARK 465 ALA B 4
REMARK 465 GLY B 5
REMARK 465 SER B 6
REMARK 465 GLU B 7
REMARK 465 LEU B 8
REMARK 465 PRO B 9
REMARK 465 ARG B 10
REMARK 465 ARG B 11
REMARK 465 PRO B 12
REMARK 465 LEU B 13
REMARK 465 PRO B 14
REMARK 465 PRO B 15
REMARK 465 ALA B 16
REMARK 465 ALA B 17
REMARK 465 GLN B 18
REMARK 465 GLU B 19
REMARK 465 ARG B 20
REMARK 465 ASP B 21
REMARK 465 ALA B 22
REMARK 465 GLU B 23
REMARK 465 PRO B 24
REMARK 465 ARG B 25
REMARK 465 ASP B 48
REMARK 465 ASP B 49
REMARK 465 GLU B 310
REMARK 465 MET B 311
REMARK 465 ALA B 312
REMARK 465 VAL B 313
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 72 77.88 -66.16
REMARK 500 LEU A 74 137.80 -32.80
REMARK 500 LYS A 77 126.65 -175.40
REMARK 500 SER A 103 24.23 -74.78
REMARK 500 PHE A 123 48.18 -107.03
REMARK 500 ASP A 130 99.37 -69.53
REMARK 500 PRO A 133 54.98 -67.93
REMARK 500 VAL A 134 -168.65 -72.05
REMARK 500 HIS A 141 48.15 -142.12
REMARK 500 ARG A 147 -79.02 -119.18
REMARK 500 MET A 149 1.45 -61.08
REMARK 500 ASN A 260 3.93 -69.38
REMARK 500 PRO A 277 -162.46 -67.73
REMARK 500 THR B 51 4.11 57.91
REMARK 500 THR B 53 -7.44 75.37
REMARK 500 THR B 55 138.96 -179.33
REMARK 500 GLU B 70 155.61 174.86
REMARK 500 LEU B 74 134.82 -32.62
REMARK 500 SER B 103 -4.78 -57.21
REMARK 500 SER B 120 2.58 -65.16
REMARK 500 PRO B 133 58.24 -68.43
REMARK 500 VAL B 134 -169.44 -79.73
REMARK 500 ARG B 147 -80.15 -119.48
REMARK 500 SER B 151 150.91 -42.92
REMARK 500 ASN B 171 57.68 -143.78
REMARK 500 PRO B 172 -7.40 -49.54
REMARK 500 CME B 195 55.62 -107.27
REMARK 500 HIS B 196 67.78 -168.46
REMARK 500 PRO B 277 -169.81 -74.54
REMARK 500 LEU B 282 -4.32 -51.91
REMARK 500 ASN B 302 75.92 -117.91
REMARK 500 PRO B 305 -179.07 -53.41
REMARK 500 ILE B 307 -90.55 -81.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 213 0.07 SIDE CHAIN
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 ANGLE, 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 CME B 195 -28.66
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 PO4 B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 655
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HVY RELATED DB: PDB
REMARK 900 RELATED ID: 1HW3 RELATED DB: PDB
REMARK 900 RELATED ID: 1YPV RELATED DB: PDB
DBREF 2RD8 A 1 313 UNP P04818 TYSY_HUMAN 1 313
DBREF 2RD8 B 1 313 UNP P04818 TYSY_HUMAN 1 313
SEQADV 2RD8 LYS A 163 UNP P04818 ARG 163 ENGINEERED MUTATION
SEQADV 2RD8 LYS B 163 UNP P04818 ARG 163 ENGINEERED MUTATION
SEQRES 1 A 313 MET PRO VAL ALA GLY SER GLU LEU PRO ARG ARG PRO LEU
SEQRES 2 A 313 PRO PRO ALA ALA GLN GLU ARG ASP ALA GLU PRO ARG PRO
SEQRES 3 A 313 PRO HIS GLY GLU LEU GLN TYR LEU GLY GLN ILE GLN HIS
SEQRES 4 A 313 ILE LEU ARG CYS GLY VAL ARG LYS ASP ASP ARG THR GLY
SEQRES 5 A 313 THR GLY THR LEU SER VAL PHE GLY MET GLN ALA ARG TYR
SEQRES 6 A 313 SER LEU ARG ASP GLU PHE PRO LEU LEU THR THR LYS ARG
SEQRES 7 A 313 VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU LEU TRP PHE
SEQRES 8 A 313 ILE LYS GLY SER THR ASN ALA LYS GLU LEU SER SER LYS
SEQRES 9 A 313 GLY VAL LYS ILE TRP ASP ALA ASN GLY SER ARG ASP PHE
SEQRES 10 A 313 LEU ASP SER LEU GLY PHE SER THR ARG GLU GLU GLY ASP
SEQRES 11 A 313 LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG HIS PHE GLY
SEQRES 12 A 313 ALA GLU TYR ARG ASP MET GLU SER ASP TYR SER GLY GLN
SEQRES 13 A 313 GLY VAL ASP GLN LEU GLN LYS VAL ILE ASP THR ILE LYS
SEQRES 14 A 313 THR ASN PRO ASP ASP ARG ARG ILE ILE MET CYS ALA TRP
SEQRES 15 A 313 ASN PRO ARG ASP LEU PRO LEU MET ALA LEU PRO PRO CYS
SEQRES 16 A 313 HIS ALA LEU CYS GLN PHE TYR VAL VAL ASN SER GLU LEU
SEQRES 17 A 313 SER CYS GLN LEU TYR GLN ARG SER GLY ASP MET GLY LEU
SEQRES 18 A 313 GLY VAL PRO PHE ASN ILE ALA SER TYR ALA LEU LEU THR
SEQRES 19 A 313 TYR MET ILE ALA HIS ILE THR GLY LEU LYS PRO GLY ASP
SEQRES 20 A 313 PHE ILE HIS THR LEU GLY ASP ALA HIS ILE TYR LEU ASN
SEQRES 21 A 313 HIS ILE GLU PRO LEU LYS ILE GLN LEU GLN ARG GLU PRO
SEQRES 22 A 313 ARG PRO PHE PRO LYS LEU ARG ILE LEU ARG LYS VAL GLU
SEQRES 23 A 313 LYS ILE ASP ASP PHE LYS ALA GLU ASP PHE GLN ILE GLU
SEQRES 24 A 313 GLY TYR ASN PRO HIS PRO THR ILE LYS MET GLU MET ALA
SEQRES 25 A 313 VAL
SEQRES 1 B 313 MET PRO VAL ALA GLY SER GLU LEU PRO ARG ARG PRO LEU
SEQRES 2 B 313 PRO PRO ALA ALA GLN GLU ARG ASP ALA GLU PRO ARG PRO
SEQRES 3 B 313 PRO HIS GLY GLU LEU GLN TYR LEU GLY GLN ILE GLN HIS
SEQRES 4 B 313 ILE LEU ARG CYS GLY VAL ARG LYS ASP ASP ARG THR GLY
SEQRES 5 B 313 THR GLY THR LEU SER VAL PHE GLY MET GLN ALA ARG TYR
SEQRES 6 B 313 SER LEU ARG ASP GLU PHE PRO LEU LEU THR THR LYS ARG
SEQRES 7 B 313 VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU LEU TRP PHE
SEQRES 8 B 313 ILE LYS GLY SER THR ASN ALA LYS GLU LEU SER SER LYS
SEQRES 9 B 313 GLY VAL LYS ILE TRP ASP ALA ASN GLY SER ARG ASP PHE
SEQRES 10 B 313 LEU ASP SER LEU GLY PHE SER THR ARG GLU GLU GLY ASP
SEQRES 11 B 313 LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG HIS PHE GLY
SEQRES 12 B 313 ALA GLU TYR ARG ASP MET GLU SER ASP TYR SER GLY GLN
SEQRES 13 B 313 GLY VAL ASP GLN LEU GLN LYS VAL ILE ASP THR ILE LYS
SEQRES 14 B 313 THR ASN PRO ASP ASP ARG ARG ILE ILE MET CYS ALA TRP
SEQRES 15 B 313 ASN PRO ARG ASP LEU PRO LEU MET ALA LEU PRO PRO CME
SEQRES 16 B 313 HIS ALA LEU CYS GLN PHE TYR VAL VAL ASN SER GLU LEU
SEQRES 17 B 313 SER CYS GLN LEU TYR GLN ARG SER GLY ASP MET GLY LEU
SEQRES 18 B 313 GLY VAL PRO PHE ASN ILE ALA SER TYR ALA LEU LEU THR
SEQRES 19 B 313 TYR MET ILE ALA HIS ILE THR GLY LEU LYS PRO GLY ASP
SEQRES 20 B 313 PHE ILE HIS THR LEU GLY ASP ALA HIS ILE TYR LEU ASN
SEQRES 21 B 313 HIS ILE GLU PRO LEU LYS ILE GLN LEU GLN ARG GLU PRO
SEQRES 22 B 313 ARG PRO PHE PRO LYS LEU ARG ILE LEU ARG LYS VAL GLU
SEQRES 23 B 313 LYS ILE ASP ASP PHE LYS ALA GLU ASP PHE GLN ILE GLU
SEQRES 24 B 313 GLY TYR ASN PRO HIS PRO THR ILE LYS MET GLU MET ALA
SEQRES 25 B 313 VAL
MODRES 2RD8 CME B 195 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME B 195 10
HET BME A 655 4
HET PO4 B 616 5
HET PO4 B 617 5
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM PO4 PHOSPHATE ION
FORMUL 2 CME C5 H11 N O3 S2
FORMUL 3 BME C2 H6 O S
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 6 HOH *88(H2 O)
HELIX 1 1 GLY A 29 GLY A 44 1 16
HELIX 2 2 PHE A 80 LYS A 93 1 14
HELIX 3 3 ASN A 97 SER A 103 1 7
HELIX 4 4 ASP A 110 GLY A 113 5 4
HELIX 5 5 SER A 114 SER A 120 1 7
HELIX 6 6 VAL A 134 PHE A 142 1 9
HELIX 7 7 ASP A 159 ASN A 171 1 13
HELIX 8 8 ASP A 186 MET A 190 5 5
HELIX 9 9 GLY A 222 THR A 241 1 20
HELIX 10 10 HIS A 261 ARG A 271 1 11
HELIX 11 11 LYS A 287 PHE A 291 5 5
HELIX 12 12 LYS A 292 GLU A 294 5 3
HELIX 13 13 GLY B 29 CYS B 43 1 15
HELIX 14 14 PHE B 80 LYS B 93 1 14
HELIX 15 15 ASN B 97 SER B 103 1 7
HELIX 16 16 ASP B 110 GLY B 113 5 4
HELIX 17 17 SER B 114 SER B 120 1 7
HELIX 18 18 VAL B 134 PHE B 142 1 9
HELIX 19 19 ASP B 159 ASN B 171 1 13
HELIX 20 20 ASP B 186 MET B 190 5 5
HELIX 21 21 GLY B 222 GLY B 242 1 21
HELIX 22 22 TYR B 258 ASN B 260 5 3
HELIX 23 23 HIS B 261 LEU B 269 1 9
HELIX 24 24 LYS B 287 PHE B 291 5 5
HELIX 25 25 LYS B 292 GLU B 294 5 3
SHEET 1 A 6 VAL A 45 ASP A 48 0
SHEET 2 A 6 GLY A 54 SER A 66 -1 O SER A 57 N VAL A 45
SHEET 3 A 6 LYS A 244 TYR A 258 -1 O ILE A 257 N LEU A 56
SHEET 4 A 6 GLU A 207 ASP A 218 1 N CYS A 210 O ILE A 249
SHEET 5 A 6 HIS A 196 VAL A 204 -1 N TYR A 202 O SER A 209
SHEET 6 A 6 ILE A 178 CYS A 180 -1 N MET A 179 O CYS A 199
SHEET 1 B 2 LYS A 278 ILE A 281 0
SHEET 2 B 2 PHE A 296 GLU A 299 -1 O GLU A 299 N LYS A 278
SHEET 1 C 5 LEU B 56 SER B 66 0
SHEET 2 C 5 LYS B 244 ILE B 257 -1 O HIS B 250 N ALA B 63
SHEET 3 C 5 GLU B 207 ASP B 218 1 N LEU B 208 O LYS B 244
SHEET 4 C 5 LEU B 198 VAL B 204 -1 N TYR B 202 O SER B 209
SHEET 5 C 5 ILE B 178 CYS B 180 -1 N MET B 179 O CYS B 199
SHEET 1 D 2 LYS B 278 ILE B 281 0
SHEET 2 D 2 PHE B 296 GLU B 299 -1 O GLU B 299 N LYS B 278
LINK C PRO B 194 N CME B 195 1555 1555 1.33
LINK C CME B 195 N HIS B 196 1555 1555 1.32
SITE 1 AC1 7 ARG A 50 ARG A 215 SER A 216 HOH A 701
SITE 2 AC1 7 ARG B 175 ARG B 176 HOH B 626
SITE 1 AC2 5 ARG A 175 ARG A 176 ARG B 50 ARG B 215
SITE 2 AC2 5 SER B 216
SITE 1 AC3 4 CYS A 195 ASP A 218 ASN A 226 HOH A 701
CRYST1 120.741 120.741 129.771 90.00 90.00 120.00 P 32 2 1 6
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 0.008282 0.004782 0.000000 0.00000
SCALE2 0.000000 0.009563 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007706 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
