HEADER TRANSFERASE 18-FEB-03 1O24
TITLE CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE COMPLEMENTING PROTEIN
TITLE 2 (TM0449) FROM THERMOTOGA MARITIMA AT 2.0 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE THYX;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: TS, TSASE, THYMIDYLATE SYNTHASE COMPLEMENTING PROTEIN;
COMPND 5 EC: 2.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: TM0449;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TM0449, THYMIDYLATE SYNTHASE COMPLEMENTING PROTEIN, STRUCTURAL
KEYWDS 2 GENOMICS, JCSG, JOINT CENTER FOR STRUCTURAL GENOMICS, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, PSI, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.I.MATHEWS,A.M.DEACON,J.M.CANAVES,D.MCMULLAN,S.A.LESLEY,S.AGARWALLA,
AUTHOR 2 P.KUHN,JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 7 20-SEP-23 1O24 1 REMARK
REVDAT 6 25-JAN-23 1O24 1 SEQADV
REVDAT 5 18-JUL-18 1O24 1 REMARK
REVDAT 4 04-OCT-17 1O24 1 REMARK
REVDAT 3 24-FEB-09 1O24 1 VERSN
REVDAT 2 14-NOV-06 1O24 1 REMARK KEYWDS AUTHOR
REVDAT 1 24-JUN-03 1O24 0
JRNL AUTH I.I.MATHEWS,A.M.DEACON,J.M.CANAVES,D.MCMULLAN,S.A.LESLEY,
JRNL AUTH 2 S.AGARWALLA,P.KUHN
JRNL TITL FUNCTIONAL ANALYSIS OF SUBSTRATE AND COFACTOR COMPLEX
JRNL TITL 2 STRUCTURES OF A THYMIDYLATE SYNTHASE-COMPLEMENTING PROTEIN
JRNL REF STRUCTURE V. 11 677 2003
JRNL REFN ISSN 0969-2126
JRNL PMID 12791256
JRNL DOI 10.1016/S0969-2126(03)00097-2
REMARK 2
REMARK 2 RESOLUTION. 2.00 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 AND HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 59344
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2996
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 : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1034
REMARK 3 BIN R VALUE (WORKING SET) : 0.2904
REMARK 3 BIN FREE R VALUE : 0.3237
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.05
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 55
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 : 7135
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 408
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.68300
REMARK 3 B22 (A**2) : 1.32100
REMARK 3 B33 (A**2) : 6.36300
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) : 0.26
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.230
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.350 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.093 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.040 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.036 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : BULK SOLVENT CORRECTION
REMARK 3 KSOL : 48.41
REMARK 3 BSOL : 0.35
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1O24 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000001708.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-02
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 : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98039
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : FLAT MIRROR,SINGLE CRYSTAL
REMARK 200 SI(311) BENT MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59761
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 46.633
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.53100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: SOLVE, RESOLVE
REMARK 200 STARTING MODEL: 1KQ4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% PEG 200, 0.1M TRIS-HCL, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 27.24000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.12600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.31950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.12600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.24000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.31950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 LEU A 35
REMARK 465 LYS A 36
REMARK 465 ASP A 37
REMARK 465 GLU A 38
REMARK 465 GLY A 89
REMARK 465 ARG A 90
REMARK 465 TYR A 91
REMARK 465 SER A 92
REMARK 465 LYS A 93
REMARK 465 LYS A 216
REMARK 465 GLU A 217
REMARK 465 VAL A 218
REMARK 465 GLN A 219
REMARK 465 VAL A 220
REMARK 465 MET B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ILE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 PHE B 31
REMARK 465 ASP B 32
REMARK 465 MET B 33
REMARK 465 GLY B 34
REMARK 465 LEU B 35
REMARK 465 LYS B 36
REMARK 465 ASP B 37
REMARK 465 MET C -11
REMARK 465 GLY C -10
REMARK 465 SER C -9
REMARK 465 ASP C -8
REMARK 465 LYS C -7
REMARK 465 ILE C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MET D -11
REMARK 465 GLY D -10
REMARK 465 SER D -9
REMARK 465 ASP D -8
REMARK 465 LYS D -7
REMARK 465 ILE D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 LYS D 36
REMARK 465 LYS D 216
REMARK 465 GLU D 217
REMARK 465 VAL D 218
REMARK 465 GLN D 219
REMARK 465 VAL D 220
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 GLU B 38 CB CG CD OE1 OE2
REMARK 470 GLU B 39 CB CG CD OE1 OE2
REMARK 470 ARG D 90 CB CG CD NE CZ NH1 NH2
REMARK 470 SER D 92 CB OG
REMARK 470 LYS D 93 CB CG 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 HIS A 0 -162.23 43.82
REMARK 500 LEU A 6 -156.90 56.53
REMARK 500 ASN A 19 -167.18 -161.95
REMARK 500 ALA A 82 172.77 179.63
REMARK 500 LEU A 106 30.58 -84.44
REMARK 500 LEU B 6 -155.97 53.69
REMARK 500 GLU B 107 131.32 -30.65
REMARK 500 LEU C 6 -150.49 59.53
REMARK 500 LYS C 8 12.04 -141.64
REMARK 500 PHE C 31 48.95 -105.76
REMARK 500 TYR C 91 -54.35 -124.50
REMARK 500 TYR C 96 72.57 51.44
REMARK 500 LEU D 6 -142.96 57.82
REMARK 500 ASN D 19 -159.80 -156.40
REMARK 500 MET D 33 -61.67 -166.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O25 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE COMPLEMENTING PROTEIN
REMARK 900 (TM0449) FROM THERMOTOGA MARITIMA WITH DUMP AT 2.4 A RESOLUTION
REMARK 900 RELATED ID: 1O26 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE COMPLEMENTING PROTEIN
REMARK 900 (TM0449) FROM THERMOTOGA MARITIMA WITH FAD AND DUMP AT 1.6 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1O27 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE COMPLEMENTING PROTEIN
REMARK 900 (TM0449) FROM THERMOTOGA MARITIMA WITH FAD AND BRDUMP AT 2.3 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1O28 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE COMPLEMENTING PROTEIN
REMARK 900 (TM0449) FROM THERMOTOGA MARITIMA WITH FDUMP AT 2.1 A RESOLUTION
REMARK 900 RELATED ID: 1O29 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE COMPLEMENTING PROTEIN
REMARK 900 (TM0449) FROM THERMOTOGA MARITIMA WITH FAD AND FDUMP AT 2.0 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1O2A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE COMPLEMENTING PROTEIN
REMARK 900 (TM0449) FROM THERMOTOGA MARITIMA WITH FAD AT 1.8 A RESOLUTION
REMARK 900 RELATED ID: 1O2B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDYLATE SYNTHASE COMPLEMENTING PROTEIN
REMARK 900 (TM0449) FROM THERMOTOGA MARITIMA WITH FAD AND PO4 AT 2.45 A
REMARK 900 RESOLUTION
DBREF 1O24 A 1 220 UNP Q9WYT0 THYX_THEMA 1 220
DBREF 1O24 B 1 220 UNP Q9WYT0 THYX_THEMA 1 220
DBREF 1O24 C 1 220 UNP Q9WYT0 THYX_THEMA 1 220
DBREF 1O24 D 1 220 UNP Q9WYT0 THYX_THEMA 1 220
SEQADV 1O24 MET A -11 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 GLY A -10 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 SER A -9 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 ASP A -8 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 LYS A -7 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 ILE A -6 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS A -5 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS A -4 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS A -3 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS A -2 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS A -1 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS A 0 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 MET B -11 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 GLY B -10 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 SER B -9 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 ASP B -8 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 LYS B -7 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 ILE B -6 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS B -5 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS B -4 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS B -3 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS B -2 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS B -1 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS B 0 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 MET C -11 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 GLY C -10 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 SER C -9 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 ASP C -8 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 LYS C -7 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 ILE C -6 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS C -5 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS C -4 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS C -3 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS C -2 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS C -1 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS C 0 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 MET D -11 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 GLY D -10 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 SER D -9 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 ASP D -8 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 LYS D -7 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 ILE D -6 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS D -5 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS D -4 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS D -3 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS D -2 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS D -1 UNP Q9WYT0 EXPRESSION TAG
SEQADV 1O24 HIS D 0 UNP Q9WYT0 EXPRESSION TAG
SEQRES 1 A 232 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 232 LYS ILE ASP ILE LEU ASP LYS GLY PHE VAL GLU LEU VAL
SEQRES 3 A 232 ASP VAL MET GLY ASN ASP LEU SER ALA VAL ARG ALA ALA
SEQRES 4 A 232 ARG VAL SER PHE ASP MET GLY LEU LYS ASP GLU GLU ARG
SEQRES 5 A 232 ASP ARG HIS LEU ILE GLU TYR LEU MET LYS HIS GLY HIS
SEQRES 6 A 232 GLU THR PRO PHE GLU HIS ILE VAL PHE THR PHE HIS VAL
SEQRES 7 A 232 LYS ALA PRO ILE PHE VAL ALA ARG GLN TRP PHE ARG HIS
SEQRES 8 A 232 ARG ILE ALA SER TYR ASN GLU LEU SER GLY ARG TYR SER
SEQRES 9 A 232 LYS LEU SER TYR GLU PHE TYR ILE PRO SER PRO GLU ARG
SEQRES 10 A 232 LEU GLU GLY TYR LYS THR THR ILE PRO PRO GLU ARG VAL
SEQRES 11 A 232 THR GLU LYS ILE SER GLU ILE VAL ASP LYS ALA TYR ARG
SEQRES 12 A 232 THR TYR LEU GLU LEU ILE GLU SER GLY VAL PRO ARG GLU
SEQRES 13 A 232 VAL ALA ARG ILE VAL LEU PRO LEU ASN LEU TYR THR ARG
SEQRES 14 A 232 PHE PHE TRP THR VAL ASN ALA ARG SER LEU MET ASN PHE
SEQRES 15 A 232 LEU ASN LEU ARG ALA ASP SER HIS ALA GLN TRP GLU ILE
SEQRES 16 A 232 GLN GLN TYR ALA LEU ALA ILE ALA ARG ILE PHE LYS GLU
SEQRES 17 A 232 LYS CYS PRO TRP THR PHE GLU ALA PHE LEU LYS TYR ALA
SEQRES 18 A 232 TYR LYS GLY ASP ILE LEU LYS GLU VAL GLN VAL
SEQRES 1 B 232 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 B 232 LYS ILE ASP ILE LEU ASP LYS GLY PHE VAL GLU LEU VAL
SEQRES 3 B 232 ASP VAL MET GLY ASN ASP LEU SER ALA VAL ARG ALA ALA
SEQRES 4 B 232 ARG VAL SER PHE ASP MET GLY LEU LYS ASP GLU GLU ARG
SEQRES 5 B 232 ASP ARG HIS LEU ILE GLU TYR LEU MET LYS HIS GLY HIS
SEQRES 6 B 232 GLU THR PRO PHE GLU HIS ILE VAL PHE THR PHE HIS VAL
SEQRES 7 B 232 LYS ALA PRO ILE PHE VAL ALA ARG GLN TRP PHE ARG HIS
SEQRES 8 B 232 ARG ILE ALA SER TYR ASN GLU LEU SER GLY ARG TYR SER
SEQRES 9 B 232 LYS LEU SER TYR GLU PHE TYR ILE PRO SER PRO GLU ARG
SEQRES 10 B 232 LEU GLU GLY TYR LYS THR THR ILE PRO PRO GLU ARG VAL
SEQRES 11 B 232 THR GLU LYS ILE SER GLU ILE VAL ASP LYS ALA TYR ARG
SEQRES 12 B 232 THR TYR LEU GLU LEU ILE GLU SER GLY VAL PRO ARG GLU
SEQRES 13 B 232 VAL ALA ARG ILE VAL LEU PRO LEU ASN LEU TYR THR ARG
SEQRES 14 B 232 PHE PHE TRP THR VAL ASN ALA ARG SER LEU MET ASN PHE
SEQRES 15 B 232 LEU ASN LEU ARG ALA ASP SER HIS ALA GLN TRP GLU ILE
SEQRES 16 B 232 GLN GLN TYR ALA LEU ALA ILE ALA ARG ILE PHE LYS GLU
SEQRES 17 B 232 LYS CYS PRO TRP THR PHE GLU ALA PHE LEU LYS TYR ALA
SEQRES 18 B 232 TYR LYS GLY ASP ILE LEU LYS GLU VAL GLN VAL
SEQRES 1 C 232 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 C 232 LYS ILE ASP ILE LEU ASP LYS GLY PHE VAL GLU LEU VAL
SEQRES 3 C 232 ASP VAL MET GLY ASN ASP LEU SER ALA VAL ARG ALA ALA
SEQRES 4 C 232 ARG VAL SER PHE ASP MET GLY LEU LYS ASP GLU GLU ARG
SEQRES 5 C 232 ASP ARG HIS LEU ILE GLU TYR LEU MET LYS HIS GLY HIS
SEQRES 6 C 232 GLU THR PRO PHE GLU HIS ILE VAL PHE THR PHE HIS VAL
SEQRES 7 C 232 LYS ALA PRO ILE PHE VAL ALA ARG GLN TRP PHE ARG HIS
SEQRES 8 C 232 ARG ILE ALA SER TYR ASN GLU LEU SER GLY ARG TYR SER
SEQRES 9 C 232 LYS LEU SER TYR GLU PHE TYR ILE PRO SER PRO GLU ARG
SEQRES 10 C 232 LEU GLU GLY TYR LYS THR THR ILE PRO PRO GLU ARG VAL
SEQRES 11 C 232 THR GLU LYS ILE SER GLU ILE VAL ASP LYS ALA TYR ARG
SEQRES 12 C 232 THR TYR LEU GLU LEU ILE GLU SER GLY VAL PRO ARG GLU
SEQRES 13 C 232 VAL ALA ARG ILE VAL LEU PRO LEU ASN LEU TYR THR ARG
SEQRES 14 C 232 PHE PHE TRP THR VAL ASN ALA ARG SER LEU MET ASN PHE
SEQRES 15 C 232 LEU ASN LEU ARG ALA ASP SER HIS ALA GLN TRP GLU ILE
SEQRES 16 C 232 GLN GLN TYR ALA LEU ALA ILE ALA ARG ILE PHE LYS GLU
SEQRES 17 C 232 LYS CYS PRO TRP THR PHE GLU ALA PHE LEU LYS TYR ALA
SEQRES 18 C 232 TYR LYS GLY ASP ILE LEU LYS GLU VAL GLN VAL
SEQRES 1 D 232 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 D 232 LYS ILE ASP ILE LEU ASP LYS GLY PHE VAL GLU LEU VAL
SEQRES 3 D 232 ASP VAL MET GLY ASN ASP LEU SER ALA VAL ARG ALA ALA
SEQRES 4 D 232 ARG VAL SER PHE ASP MET GLY LEU LYS ASP GLU GLU ARG
SEQRES 5 D 232 ASP ARG HIS LEU ILE GLU TYR LEU MET LYS HIS GLY HIS
SEQRES 6 D 232 GLU THR PRO PHE GLU HIS ILE VAL PHE THR PHE HIS VAL
SEQRES 7 D 232 LYS ALA PRO ILE PHE VAL ALA ARG GLN TRP PHE ARG HIS
SEQRES 8 D 232 ARG ILE ALA SER TYR ASN GLU LEU SER GLY ARG TYR SER
SEQRES 9 D 232 LYS LEU SER TYR GLU PHE TYR ILE PRO SER PRO GLU ARG
SEQRES 10 D 232 LEU GLU GLY TYR LYS THR THR ILE PRO PRO GLU ARG VAL
SEQRES 11 D 232 THR GLU LYS ILE SER GLU ILE VAL ASP LYS ALA TYR ARG
SEQRES 12 D 232 THR TYR LEU GLU LEU ILE GLU SER GLY VAL PRO ARG GLU
SEQRES 13 D 232 VAL ALA ARG ILE VAL LEU PRO LEU ASN LEU TYR THR ARG
SEQRES 14 D 232 PHE PHE TRP THR VAL ASN ALA ARG SER LEU MET ASN PHE
SEQRES 15 D 232 LEU ASN LEU ARG ALA ASP SER HIS ALA GLN TRP GLU ILE
SEQRES 16 D 232 GLN GLN TYR ALA LEU ALA ILE ALA ARG ILE PHE LYS GLU
SEQRES 17 D 232 LYS CYS PRO TRP THR PHE GLU ALA PHE LEU LYS TYR ALA
SEQRES 18 D 232 TYR LYS GLY ASP ILE LEU LYS GLU VAL GLN VAL
FORMUL 5 HOH *408(H2 O)
HELIX 1 1 ASN A 19 VAL A 29 1 11
HELIX 2 2 GLU A 39 HIS A 51 1 13
HELIX 3 3 GLU A 54 HIS A 59 5 6
HELIX 4 4 ILE A 70 PHE A 77 1 8
HELIX 5 5 SER A 102 GLU A 107 5 6
HELIX 6 6 PRO A 114 SER A 139 1 26
HELIX 7 7 PRO A 142 ARG A 147 1 6
HELIX 8 8 ILE A 148 LEU A 150 5 3
HELIX 9 9 ALA A 164 ALA A 175 1 12
HELIX 10 10 GLN A 180 CYS A 198 1 19
HELIX 11 11 CYS A 198 ALA A 209 1 12
HELIX 12 12 ASN B 19 VAL B 29 1 11
HELIX 13 13 GLU B 38 HIS B 51 1 14
HELIX 14 14 GLU B 54 HIS B 59 5 6
HELIX 15 15 ILE B 70 PHE B 77 1 8
HELIX 16 16 SER B 102 GLU B 107 1 6
HELIX 17 17 PRO B 114 SER B 139 1 26
HELIX 18 18 PRO B 142 ARG B 147 1 6
HELIX 19 19 ILE B 148 LEU B 150 5 3
HELIX 20 20 ALA B 164 ALA B 175 1 12
HELIX 21 21 GLN B 180 CYS B 198 1 19
HELIX 22 22 CYS B 198 ALA B 209 1 12
HELIX 23 23 ASP B 213 GLU B 217 5 5
HELIX 24 24 ASN C 19 VAL C 29 1 11
HELIX 25 25 ASP C 37 HIS C 51 1 15
HELIX 26 26 GLU C 54 HIS C 59 5 6
HELIX 27 27 ILE C 70 PHE C 77 1 8
HELIX 28 28 SER C 102 GLU C 107 1 6
HELIX 29 29 PRO C 114 GLU C 138 1 25
HELIX 30 30 PRO C 142 ARG C 147 1 6
HELIX 31 31 ILE C 148 LEU C 150 5 3
HELIX 32 32 ALA C 164 ALA C 175 1 12
HELIX 33 33 GLN C 180 CYS C 198 1 19
HELIX 34 34 CYS C 198 ALA C 209 1 12
HELIX 35 35 ASP C 213 VAL C 218 1 6
HELIX 36 36 ASN D 19 VAL D 29 1 11
HELIX 37 37 ASP D 37 GLY D 52 1 16
HELIX 38 38 GLU D 54 HIS D 59 5 6
HELIX 39 39 ILE D 70 PHE D 77 1 8
HELIX 40 40 SER D 102 GLU D 107 5 6
HELIX 41 41 PRO D 114 SER D 139 1 26
HELIX 42 42 PRO D 142 ARG D 147 1 6
HELIX 43 43 ILE D 148 LEU D 150 5 3
HELIX 44 44 ALA D 164 ALA D 175 1 12
HELIX 45 45 GLN D 180 CYS D 198 1 19
HELIX 46 46 CYS D 198 ALA D 209 1 12
SHEET 1 A 5 LYS A 2 ILE A 5 0
SHEET 2 A 5 GLY A 9 MET A 17 -1 O VAL A 11 N ILE A 3
SHEET 3 A 5 VAL A 61 PRO A 69 -1 O VAL A 61 N MET A 17
SHEET 4 A 5 TYR A 155 ASN A 163 -1 O PHE A 158 N VAL A 66
SHEET 5 A 5 SER A 83 GLU A 86 -1 N SER A 83 O THR A 161
SHEET 1 B 5 LYS B 2 ILE B 5 0
SHEET 2 B 5 GLY B 9 MET B 17 -1 O VAL B 11 N ILE B 3
SHEET 3 B 5 VAL B 61 PRO B 69 -1 O HIS B 65 N GLU B 12
SHEET 4 B 5 TYR B 155 ASN B 163 -1 O TRP B 160 N PHE B 64
SHEET 5 B 5 SER B 83 GLU B 86 -1 N SER B 83 O THR B 161
SHEET 1 C 5 LYS C 2 ILE C 5 0
SHEET 2 C 5 GLY C 9 MET C 17 -1 O VAL C 11 N ILE C 3
SHEET 3 C 5 VAL C 61 PRO C 69 -1 O VAL C 61 N MET C 17
SHEET 4 C 5 TYR C 155 ASN C 163 -1 O THR C 156 N ALA C 68
SHEET 5 C 5 SER C 83 GLU C 86 -1 N SER C 83 O THR C 161
SHEET 1 D 5 LYS D 2 ILE D 5 0
SHEET 2 D 5 GLY D 9 MET D 17 -1 O VAL D 11 N ILE D 3
SHEET 3 D 5 VAL D 61 PRO D 69 -1 O VAL D 61 N MET D 17
SHEET 4 D 5 TYR D 155 ASN D 163 -1 O PHE D 158 N VAL D 66
SHEET 5 D 5 SER D 83 GLU D 86 -1 N SER D 83 O THR D 161
CRYST1 54.480 116.639 142.252 90.00 90.00 90.00 P 21 21 21 16
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 0.018355 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008573 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007030 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
