BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27744

Title: Backbone chemical shift assignments of translation initiation factor 3 from Pseudomonas aeruginosa   PubMed: 31902070

Deposition date: 2018-12-26 Original release date: 2020-02-28

Authors: Zhang, Yonghong

Citation: Li, Libo; Palmer, Stephanie; Gomez, Elizabeth; Mendiola, Frank; Wang, Tianzhi; Bullard, James; Zhang, Yonghong. "Backbone chemical shift assignments of translation initiation factor 3 from Pseudomonas aeruginosa"  Biomol. NMR Assignments 14, 93-97 (2020).

Assembly members:
PaIF3, polymer, 193 residues, Formula weight is not available

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

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

Entity Sequences (FASTA):
PaIF3: MASIIKREMRQDKRAQPKPP INENISAREVRLIGADGQQV GVVSIDEAIRLAEEAKLDLV EISADAVPPVCRIMDYGKHL FEKKKQAAVAKKNQKQAQVK EIKFRPGTEEGDYQVKLRNL VRFLSEGDKAKVSLRFRGRE MAHQELGMELLKRVEADLVE YGTVEQHPKLEGRQLMMVIA PKKKKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts677
15N chemical shifts171
1H chemical shifts1145

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PaIF31

Entities:

Entity 1, PaIF3 193 residues - Formula weight is not available

The first three residues (MAS) are from cloning artifacts. The last 8 residues (LEHHHHHH) represent a non-native affinity tag. This is a bacterial ribosome binding protein from Pseudomonas aeruginosa.

1   METALASERILEILELYSARGGLUMETARG
2   GLNASPLYSARGALAGLNPROLYSPROPRO
3   ILEASNGLUASNILESERALAARGGLUVAL
4   ARGLEUILEGLYALAASPGLYGLNGLNVAL
5   GLYVALVALSERILEASPGLUALAILEARG
6   LEUALAGLUGLUALALYSLEUASPLEUVAL
7   GLUILESERALAASPALAVALPROPROVAL
8   CYSARGILEMETASPTYRGLYLYSHISLEU
9   PHEGLULYSLYSLYSGLNALAALAVALALA
10   LYSLYSASNGLNLYSGLNALAGLNVALLYS
11   GLUILELYSPHEARGPROGLYTHRGLUGLU
12   GLYASPTYRGLNVALLYSLEUARGASNLEU
13   VALARGPHELEUSERGLUGLYASPLYSALA
14   LYSVALSERLEUARGPHEARGGLYARGGLU
15   METALAHISGLNGLULEUGLYMETGLULEU
16   LEULYSARGVALGLUALAASPLEUVALGLU
17   TYRGLYTHRVALGLUGLNHISPROLYSLEU
18   GLUGLYARGGLNLEUMETMETVALILEALA
19   PROLYSLYSLYSLYSLEUGLUHISHISHIS
20   HISHISHIS

Samples:

sample_1: PaIF3, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 25 mM; sodium chloride 25 mM; dithiothreitol-d10 10 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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