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- PDB-1t6r: Solution structure of TM1442, a putative anti sigma factor antago... -

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Basic information

Entry
Database: PDB / ID: 1t6r
TitleSolution structure of TM1442, a putative anti sigma factor antagonist in phosphorylated state
ComponentsPutative anti-sigma factor antagonist TM1442
KeywordsSTRUCTURAL GENOMICS / UNKNOWN FUNCTION / Phosphorylation / solution structure / PSI / Protein Structure Initiative / Joint Center for Structural Genomics / JCSG
Function / homology
Function and homology information


anti-sigma factor antagonist activity
Similarity search - Function
Anti-sigma factor antagonist / STAS domain / Transcription Regulator spoIIAA / STAS domain / STAS domain profile. / STAS domain / STAS domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Putative anti-sigma factor antagonist TM_1442
Similarity search - Component
Biological speciesThermotoga maritima (bacteria)
MethodSOLUTION NMR
AuthorsEtezady-Esfarjani, T. / Placzek, W. / Herrmann, T. / Lesley, S.A. / Wuthrich, K. / Joint Center for Structural Genomics (JCSG)
CitationJournal: Magn.Reson.Chem. / Year: 2006
Title: Solution structures of the putative anti-sigma-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states.
Authors: Etezady-Esfarjani, T. / Placzek, W.J. / Herrmann, T. / Wuthrich, K.
History
DepositionMay 7, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 24, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Putative anti-sigma factor antagonist TM1442


Theoretical massNumber of molelcules
Total (without water)12,3971
Polymers12,3971
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with acceptable covalent geometry
RepresentativeModel #1closest to the average

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Components

#1: Protein Putative anti-sigma factor antagonist TM1442


Mass: 12397.194 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermotoga maritima (bacteria) / Gene: TM1442 / Plasmid: pET25b(+) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q9X1F5

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
2223D 15N-separated NOESY
3333D 13C-separated NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
12mM TM1442, 90% H2O, 10% D2O90% H2O/10% D2O
21.5mM 15N-TM1442, 90% H2O, 10% D2O90% H2O/10% D2O
31.5mM 15N,13C-TM1442, 90% H2O, 10% D2O90% H2O/10% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
120 mM sodiumphosphate 7.0 ambient 313 K
220 mM sodiumphosphate 7.0 ambient 313 K
320 mM sodiumphosphate 7.0 ambient 313 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE6001
Bruker AVANCEBrukerAVANCE9002

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Processing

NMR software
NameVersionClassification
XwinNMR3.5collection
DYANA6data analysis
XEASY1data analysis
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with acceptable covalent geometry
Conformers calculated total number: 100 / Conformers submitted total number: 20

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