BMRB Entry 25856

Title:
Solution structure of translation initiation factor from Staphylococcus aureus Mu50   PubMed: 27784646
Deposition date:
2015-10-21
Original release date:
2016-10-20
Authors:
Kim, Do-Hee; Lee, Ki-Young; Lee, Bong-Jin
Citation:

Citation: Kim, Do-Hee; Kang, Su-Jin; Lee, Ki-Young; Jang, Sun-Bok; Kang, Sung-Min; Lee, Bong-Jin. "Structure and dynamics study of translation initiation factor 1 from Staphylococcus aureus suggests its RNA binding mode."  Biochim. Biophys. Acta 1865, 65-75 (2017).

Assembly members:

Assembly members:
Translation_factor, polymer, 72 residues, 8291.713 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 1388021   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Experimental source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 1388021   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts269
15N chemical shifts65
1H chemical shifts378

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Translation_factor1

Entities:

Entity 1, Translation_factor 72 residues - 8291.713 Da.

1   METALALYSGLNASPVALILEGLULEUGLU
2   GLYTHRVALLEUASPTHRLEUPROASNALA
3   METPHELYSVALGLULEUGLUASNGLYHIS
4   GLUILELEUALAHISVALSERGLYLYSILE
5   ARGMETASNTYRILEARGILELEUPROGLY
6   ASPLYSVALTHRVALGLUMETSERPROTYR
7   ASPLEUTHRARGGLYARGILETHRTYRARG
8   TYRLYS

Samples:

sample_1: PMSF 0.1 mM; EDTA 1 mM; sodium chloride 50 mM; MES 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

UNP P65118

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts