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 28087

Title: dUnr Cterminal Qrich   PubMed: 32697992

Deposition date: 2020-02-18 Original release date: 2021-09-21

Authors: Hollmann, Nele Merret; Hennig, Janosch

Citation: Hollmann, Nele Merret; Jagtap, Pravin Kumar Ankush; Masiewicz, Pawel; Guitart, Tanit; Simon, Bernd; Provaznik, Jan; Stein, Frank; Haberkant, Per; Sweetapple, Lara Jayne; Villacorte, Laura; Mooijman, Dylan; Benes, Valdimir; Savitski, Mikhail; Gebauer, Fatima; Hennig, Janosch. "Pseudo-RNA binding domains mediate RNA structure specificity in Upstream of N-Ras"  Cell Rep. 32, 107930-107930 (2020).

Assembly members:
dUNR_Cterminal_Q-rich, polymer, 85 residues, 8777.16 Da.

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-11

Entity Sequences (FASTA):
dUNR_Cterminal_Q-rich: GQQQQQQQQQLHLNQSNAGA NINQNDQLGGLSNGISSSSS NASLQNGYVMHGSPGGSTSS VGSNNPVHLDEFKMENNNHA GSDAG

Data sets:
Data typeCount
13C chemical shifts116
15N chemical shifts64
1H chemical shifts64

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1dUnr Cterminal Q-rich1

Entities:

Entity 1, dUnr Cterminal Q-rich 85 residues - 8777.16 Da.

The first residue (G) is a leftover from the cleavage site and not part of the native protein sequence.

1   GLYGLNGLNGLNGLNGLNGLNGLNGLNGLN
2   LEUHISLEUASNGLNSERASNALAGLYALA
3   ASNILEASNGLNASNASPGLNLEUGLYGLY
4   LEUSERASNGLYILESERSERSERSERSER
5   ASNALASERLEUGLNASNGLYTYRVALMET
6   HISGLYSERPROGLYGLYSERTHRSERSER
7   VALGLYSERASNASNPROVALHISLEUASP
8   GLUPHELYSMETGLUASNASNASNHISALA
9   GLYSERASPALAGLY

Samples:

sample_1: dUNR Cterminal Q-rich, [U-99% 13C; U-99% 15N], 0.1 mM; sodium chloride 50 mM; sodium phosphate 20 mM; DTT 1 mM

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

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

TOPSPIN, Bruker Biospin - collection

Cara, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance III 800 MHz

Related Database Links:

UNP Q9VSK3
AlphaFold Q9VSK3

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