HEADER TRANSFERASE 19-JUL-12 4G6W
TITLE HUMAN THYMIDYLATE SYNTHASE M190K WITH BOUND 4-BROMOBENZENE-1,2,3-TRIOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: X;
COMPND 4 EC: 2.1.1.45;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TYMS, TS, OK/SW-CL.29;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TX61-;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTSO80
KEYWDS METHYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.R.CELESTE,L.LEBIODA
REVDAT 3 13-SEP-23 4G6W 1 REMARK SEQADV LINK
REVDAT 2 19-NOV-14 4G6W 1 HET HETATM HETNAM LINK
REVDAT 2 2 1 MODRES SEQRES
REVDAT 1 24-JUL-13 4G6W 0
JRNL AUTH L.R.CELESTE,L.L.LOVELACE,L.LEBIODA
JRNL TITL OXIDATION OF CYSTEINE 195 OF HUYMAN THYMIDYLATE SYNTHASE BY
JRNL TITL 2 PURPUROGALLIN
JRNL REF TO BE PUBLISHED 2012
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 18295
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 933
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1261
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2135
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 67
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.79000
REMARK 3 B22 (A**2) : -1.79000
REMARK 3 B33 (A**2) : 2.68000
REMARK 3 B12 (A**2) : -0.89000
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): 0.189
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.225
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.000
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.006
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.40
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4G6W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073813.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 1.0
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19433
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 94.3
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.42200
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: 3EHI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 7.5-8.5, 20 MM BME, 25
REMARK 280 -42% AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 278K, PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 26.84167
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 53.68333
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 53.68333
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 26.84167
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 53.68333
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 O1 PBX X 600 LIES ON A SPECIAL POSITION.
REMARK 375 C5 PBX X 600 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 MET X 1
REMARK 465 PRO X 2
REMARK 465 VAL X 3
REMARK 465 ALA X 4
REMARK 465 GLY X 5
REMARK 465 SER X 6
REMARK 465 GLU X 7
REMARK 465 LEU X 8
REMARK 465 PRO X 9
REMARK 465 ARG X 10
REMARK 465 ARG X 11
REMARK 465 PRO X 12
REMARK 465 LEU X 13
REMARK 465 PRO X 14
REMARK 465 PRO X 15
REMARK 465 ALA X 16
REMARK 465 ALA X 17
REMARK 465 GLN X 18
REMARK 465 GLU X 19
REMARK 465 ARG X 20
REMARK 465 ASP X 21
REMARK 465 ALA X 22
REMARK 465 GLU X 23
REMARK 465 PRO X 24
REMARK 465 ARG X 25
REMARK 465 PRO X 26
REMARK 465 SER X 103
REMARK 465 LYS X 104
REMARK 465 GLY X 105
REMARK 465 VAL X 106
REMARK 465 LYS X 107
REMARK 465 ILE X 108
REMARK 465 TRP X 109
REMARK 465 ASP X 110
REMARK 465 ALA X 111
REMARK 465 ASN X 112
REMARK 465 GLY X 113
REMARK 465 SER X 114
REMARK 465 ARG X 115
REMARK 465 ASP X 116
REMARK 465 MET X 311
REMARK 465 ALA X 312
REMARK 465 VAL X 313
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 X 82 CG CD CE NZ
REMARK 470 LYS X 93 CE NZ
REMARK 470 LYS X 99 CG CD CE NZ
REMARK 470 LEU X 101 CG CD1 CD2
REMARK 470 PHE X 117 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU X 127 CG CD OE1 OE2
REMARK 470 GLU X 145 CG CD OE1 OE2
REMARK 470 ARG X 147 CD NE CZ NH1 NH2
REMARK 470 ASP X 148 CG OD1 OD2
REMARK 470 GLU X 150 CG CD OE1 OE2
REMARK 470 LYS X 190 CG CD CE NZ
REMARK 470 LYS X 244 CG CD CE NZ
REMARK 470 LYS X 284 CD CE NZ
REMARK 470 LYS X 287 CD CE NZ
REMARK 470 LYS X 292 CD CE NZ
REMARK 470 GLU X 294 CD OE1 OE2
REMARK 470 LYS X 308 CD CE NZ
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 PHE X 80 72.49 -69.04
REMARK 500 ASP X 119 106.98 -51.30
REMARK 500 SER X 120 122.43 -172.44
REMARK 500 LEU X 121 108.52 -167.34
REMARK 500 PHE X 123 -82.22 -114.52
REMARK 500 GLU X 128 -39.94 -36.74
REMARK 500 TYR X 135 -128.04 55.33
REMARK 500 HIS X 141 47.20 -147.54
REMARK 500 ARG X 147 -97.96 -97.50
REMARK 500 LEU X 189 -21.23 86.52
REMARK 500 ALA X 191 -2.13 -53.92
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 PBX X 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 X 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 X 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EHI RELATED DB: PDB
REMARK 900 SAME STRUCTURE WITH NO LIGANDS
REMARK 900 RELATED ID: 4G2O RELATED DB: PDB
REMARK 900 SAME STRUCTURE WITH PURPUROGALLIN BOUND
REMARK 900 RELATED ID: 4GD7 RELATED DB: PDB
DBREF 4G6W X 1 313 UNP P04818 TYSY_HUMAN 1 313
SEQADV 4G6W LYS X 190 UNP P04818 MET 190 ENGINEERED MUTATION
SEQRES 1 X 313 MET PRO VAL ALA GLY SER GLU LEU PRO ARG ARG PRO LEU
SEQRES 2 X 313 PRO PRO ALA ALA GLN GLU ARG ASP ALA GLU PRO ARG PRO
SEQRES 3 X 313 PRO HIS GLY GLU LEU GLN TYR LEU GLY GLN ILE GLN HIS
SEQRES 4 X 313 ILE LEU ARG CYS GLY VAL ARG LYS ASP ASP ARG THR GLY
SEQRES 5 X 313 THR GLY THR LEU SER VAL PHE GLY MET GLN ALA ARG TYR
SEQRES 6 X 313 SER LEU ARG ASP GLU PHE PRO LEU LEU THR THR LYS ARG
SEQRES 7 X 313 VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU LEU TRP PHE
SEQRES 8 X 313 ILE LYS GLY SER THR ASN ALA LYS GLU LEU SER SER LYS
SEQRES 9 X 313 GLY VAL LYS ILE TRP ASP ALA ASN GLY SER ARG ASP PHE
SEQRES 10 X 313 LEU ASP SER LEU GLY PHE SER THR ARG GLU GLU GLY ASP
SEQRES 11 X 313 LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG HIS PHE GLY
SEQRES 12 X 313 ALA GLU TYR ARG ASP MET GLU SER ASP TYR SER GLY GLN
SEQRES 13 X 313 GLY VAL ASP GLN LEU GLN ARG VAL ILE ASP THR ILE LYS
SEQRES 14 X 313 THR ASN PRO ASP ASP ARG ARG ILE ILE MET CME ALA TRP
SEQRES 15 X 313 ASN PRO ARG ASP LEU PRO LEU LYS ALA LEU PRO PRO CSD
SEQRES 16 X 313 HIS ALA LEU CYS GLN PHE TYR VAL VAL ASN SER GLU LEU
SEQRES 17 X 313 SER CYS GLN LEU TYR GLN ARG SER GLY ASP MET GLY LEU
SEQRES 18 X 313 GLY VAL PRO PHE ASN ILE ALA SER TYR ALA LEU LEU THR
SEQRES 19 X 313 TYR MET ILE ALA HIS ILE THR GLY LEU LYS PRO GLY ASP
SEQRES 20 X 313 PHE ILE HIS THR LEU GLY ASP ALA HIS ILE TYR LEU ASN
SEQRES 21 X 313 HIS ILE GLU PRO LEU LYS ILE GLN LEU GLN ARG GLU PRO
SEQRES 22 X 313 ARG PRO PHE PRO LYS LEU ARG ILE LEU ARG LYS VAL GLU
SEQRES 23 X 313 LYS ILE ASP ASP PHE LYS ALA GLU ASP PHE GLN ILE GLU
SEQRES 24 X 313 GLY TYR ASN PRO HIS PRO THR ILE LYS MET GLU MET ALA
SEQRES 25 X 313 VAL
MODRES 4G6W CME X 180 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 4G6W CSD X 195 CYS 3-SULFINOALANINE
HET CME X 180 10
HET CSD X 195 8
HET PBX X 600 10
HET SO4 X 601 5
HET SO4 X 602 5
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM CSD 3-SULFINOALANINE
HETNAM PBX 4-BROMOBENZENE-1,2,3-TRIOL
HETNAM SO4 SULFATE ION
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CME C5 H11 N O3 S2
FORMUL 1 CSD C3 H7 N O4 S
FORMUL 2 PBX C6 H5 BR O3
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *67(H2 O)
HELIX 1 1 GLY X 29 GLY X 44 1 16
HELIX 2 2 PHE X 80 GLY X 94 1 15
HELIX 3 3 ASN X 97 SER X 102 1 6
HELIX 4 4 PHE X 123 GLY X 129 1 7
HELIX 5 5 TYR X 135 HIS X 141 1 7
HELIX 6 6 ASP X 159 ASN X 171 1 13
HELIX 7 7 ASN X 183 LEU X 187 5 5
HELIX 8 8 LEU X 221 THR X 241 1 21
HELIX 9 9 HIS X 261 LEU X 269 1 9
HELIX 10 10 LYS X 287 PHE X 291 5 5
HELIX 11 11 LYS X 292 GLU X 294 5 3
SHEET 1 A 6 VAL X 45 ASP X 48 0
SHEET 2 A 6 GLY X 54 SER X 66 -1 O SER X 57 N VAL X 45
SHEET 3 A 6 LYS X 244 TYR X 258 -1 O HIS X 250 N ALA X 63
SHEET 4 A 6 GLU X 207 ASP X 218 1 N LEU X 208 O GLY X 246
SHEET 5 A 6 ALA X 197 VAL X 204 -1 N TYR X 202 O SER X 209
SHEET 6 A 6 ILE X 178 ALA X 181 -1 N MET X 179 O CYS X 199
SHEET 1 B 2 LYS X 278 ILE X 281 0
SHEET 2 B 2 PHE X 296 GLU X 299 -1 O GLN X 297 N ARG X 280
LINK C MET X 179 N CME X 180 1555 1555 1.33
LINK C CME X 180 N ALA X 181 1555 1555 1.35
LINK C PRO X 194 N CSD X 195 1555 1555 1.36
LINK C CSD X 195 N HIS X 196 1555 1555 1.32
SITE 1 AC1 5 CME X 180 TRP X 182 LEU X 189 LEU X 192
SITE 2 AC1 5 PRO X 193
SITE 1 AC2 6 ARG X 78 ARG X 176 ARG X 185 PRO X 305
SITE 2 AC2 6 THR X 306 HOH X 745
SITE 1 AC3 6 ARG X 175 ASN X 183 ARG X 185 ARG X 215
SITE 2 AC3 6 SER X 216 HOH X 712
CRYST1 95.846 95.846 80.525 90.00 90.00 120.00 P 31 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 0.010433 0.006024 0.000000 0.00000
SCALE2 0.000000 0.012047 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012419 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
