BMRB Entry 52359

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52359

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Title:
Backbone assignment of Hrp48 RRM1
Deposition date:
2024-03-21
Original release date:
2024-12-26
Authors:
Lomoschitz, Andrea; Meyer, Julia; Schweimer, Kristian; Hennig, Janosch
Citation:

Citation: Lomoschitz, Andrea; Meyer, Julia; Guitart, Tanit; Krepl, Miroslav; Lapouge, Karine; Hayn, Clara; Schweimer, Kristian; Simon, Bernd; Sponer, Jiri; Gebauer, Fatima; Hennig, Janosch. "The Drosophila RNA binding protein Hrp48 binds a specific RNA sequence of the msl-2 mRNA 3' UTR to regulate translation"  Biophys. Chem. 316, 107346-107346 (2025).
PubMed: 39504588

Assembly members:

Assembly members:
entity_1, polymer, 90 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMEEDERGKLFVGGLSWET TQENLSRYFCRFGDIIDCVV MKNNESGRSRGFGFVTFADP TNVNHVLQNGPHTLDGRTID PKPCNPRTLQ

Data sets:
Data typeCount
13C chemical shifts164
15N chemical shifts83
1H chemical shifts83

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Hrp48 RRM11

Entities:

Entity 1, Hrp48 RRM1 90 residues - Formula weight is not available

N-terminal GA from expression tag

1   GLYALAMETGLUGLUASPGLUARGGLYLYS
2   LEUPHEVALGLYGLYLEUSERTRPGLUTHR
3   THRGLNGLUASNLEUSERARGTYRPHECYS
4   ARGPHEGLYASPILEILEASPCYSVALVAL
5   METLYSASNASNGLUSERGLYARGSERARG
6   GLYPHEGLYPHEVALTHRPHEALAASPPRO
7   THRASNVALASNHISVALLEUGLNASNGLY
8   PROHISTHRLEUASPGLYARGTHRILEASP
9   PROLYSPROCYSASNPROARGTHRLEUGLN

Samples:

sample_1: Hrp48 RRM1, [U-95% 13C; U-95% 15N], 500 uM; MES 20 mM; sodium chloride 200 mM; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 0.4 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CARA - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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