BMRB Entry 19499

Title:
HuR RRM3 W261E mutant
Deposition date:
2013-09-16
Original release date:
2015-02-05
Authors:
Blanco, Francisco; Scheiba, Rafael; Ibanez de Opakua, Alain
Citation:

Citation: Scheiba, Rafael; Ibanez de Opakua, Alain; Diaz-Quintana, Antonio; Cruz-Gallardo, Isabel; Martinez-Cruz, Luis; Martinez-Chantar, Maria; Blanco, Francisco; Diaz-Moreno, Irene. "The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets"  RNA Biol. 11, 1250-1261 (2014).
PubMed: 25584704

Assembly members:

Assembly members:
HUR_RRM3_W261E_mutant, polymer, 124 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET M11

Data sets:
Data typeCount
13C chemical shifts297
15N chemical shifts118
1H chemical shifts246

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HUR RRM3 W261E mutant1

Entities:

Entity 1, HUR RRM3 W261E mutant 124 residues - Formula weight is not available

Residues 1-41 represent a non-native linker with an affinity tag

1   METLYSHISHISHISHISHISHISPROMET
2   SERASPTYRASPILEPROTHRTHRGLUILE
3   SERGLYARGGLUASNLEUTYRPHEGLNSER
4   GLYSERGLUPHEPROALAGLUTHRPROSER
5   GLYTRPCYSILEPHEILETYRASNLEUGLY
6   GLNASPALAASPGLUGLYILELEUGLUGLN
7   METPHEGLYPROPHEGLYALAVALTHRASN
8   VALLYSVALILEARGASPPHEASNTHRASN
9   LYSCYSLYSGLYPHEGLYPHEVALTHRMET
10   THRASNTYRGLUGLUALAALAMETALAILE
11   ALASERLEUASNGLYTYRARGLEUGLYASP
12   LYSILELEUGLNVALSERPHELYSTHRASN
13   LYSSERHISLYS

Samples:

sample_1: HUR RRM3 W261E mutant, [U-99% 13C; U-99% 15N], 80 uM; DTT 3 mM; D2O 5%; sodium azide 0.02%; DSS 30 uM; sodium phosphate 10 mM

sample_conditions_1: pH: 7.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(COCA)HAsample_1isotropicsample_conditions_1
3D HN(CA)HAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - data analysis, peak picking

MARS, (MARS) Zweckstetter - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19494 19500

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