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- PDB-1gh9: SOLUTION STRUCTURE OF A 8.3 KDA PROTEIN (GENE MTH1184) FROM METHA... -

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Basic information

Entry
Database: PDB / ID: 1gh9
TitleSOLUTION STRUCTURE OF A 8.3 KDA PROTEIN (GENE MTH1184) FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
Components8.3 KDA PROTEIN (GENE MTH1184)
KeywordsSTRUCTURAL GENOMICS / UNKNOWN FUNCTION / BETA+ALPHA COMPLEX STRUCTURE / PSI / Protein Structure Initiative / Northeast Structural Genomics Consortium / NESG
Function / homologyProtein of unknown function DUF1922 / Hypothetical protein MTH1184 / Domain of unknown function (DUF1922) / Rubredoxin-like / Structural Genomics, Unknown Function 30-nov-00 1gh9 Mol_id / Alpha-Beta Complex / Alpha Beta / Protein MTH_1184
Function and homology information
Biological speciesMethanothermobacter thermautotrophicus (archaea)
MethodSOLUTION NMR / simulated annealing
AuthorsKozlov, G. / Ekiel, I. / Gehring, K. / Northeast Structural Genomics Consortium (NESG)
CitationJournal: Nat.Struct.Biol. / Year: 2000
Title: Structural proteomics of an archaeon.
Authors: Christendat, D. / Yee, A. / Dharamsi, A. / Kluger, Y. / Savchenko, A. / Cort, J.R. / Booth, V. / Mackereth, C.D. / Saridakis, V. / Ekiel, I. / Kozlov, G. / Maxwell, K.L. / Wu, N. / McIntosh, ...Authors: Christendat, D. / Yee, A. / Dharamsi, A. / Kluger, Y. / Savchenko, A. / Cort, J.R. / Booth, V. / Mackereth, C.D. / Saridakis, V. / Ekiel, I. / Kozlov, G. / Maxwell, K.L. / Wu, N. / McIntosh, L.P. / Gehring, K. / Kennedy, M.A. / Davidson, A.R. / Pai, E.F. / Gerstein, M. / Edwards, A.M. / Arrowsmith, C.H.
History
DepositionNov 30, 2000Deposition site: RCSB / Processing site: RCSB
SupersessionDec 11, 2000ID: 1DW7
Revision 1.0Dec 11, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: 8.3 KDA PROTEIN (GENE MTH1184)


Theoretical massNumber of molelcules
Total (without water)8,3431
Polymers8,3431
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 50structures with the lowest energy
RepresentativeModel #1

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Components

#1: Protein 8.3 KDA PROTEIN (GENE MTH1184)


Mass: 8342.562 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Methanothermobacter thermautotrophicus (archaea)
Gene: MTH1184 / Plasmid: PET15B / Production host: Escherichia coli (E. coli) / References: UniProt: O27252

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-SEPARATED NOESY
1213D 15N-SEPARATED NOESY
131HNHA
1412D NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING BOTH TRIPLE- RESONANCE AND HOMONUCLEAR TECHNIQUES.

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Sample preparation

DetailsContents: 1-2MM PROTEIN 15N,13C 50MM PHOSPHATE BUFFER; 0.15M NACL; 1MM DTT
Sample conditionsIonic strength: 0.15 / pH: 6.3 / Pressure: AMBIENT / Temperature: 305.00 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz

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Processing

NMR software
NameVersionClassification
XwinNMR2.1structure solution
GIFA V.4V.4structure solution
XEASY1.3.13structure solution
CNS0.5structure solution
ARIA0.1structure solution
ARIA0.1refinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: THE STRUCTURES ARE BASED ON A TOTAL OF 950 RESTRAINTS INCLUDING 317 INTRARESIDUAL, 217 SEQUENTIAL, 92 MEDIUM, AND 236 LONG-RANGE NOES, 62 DIHEDRAL PHI ANGLES, AND 26 HYDROGEN BONDS.
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 50 / Conformers submitted total number: 20

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