BMRB Entry 25244

Title:
1H, 15N and 13C resonance assignments of the RRM1 domain of the key post-transcriptional regulator HuR
Deposition date:
2014-09-23
Original release date:
2015-09-04
Authors:
Mujo, Amanda; Lixa, Carolina; Anobom, Cristiane; Almeida, Fabio; Pinheiro, Anderson
Citation:

Citation: Mujo, Amanda; Lixa, Carolina; Carneiro, Letcia; Anobom, Cristiane; Almeida, Fabio; Pinheiro, Anderson. "1H, 15N and 13C resonance assignments of the RRM1 domain of the key post-transcriptional regulator HuR"  Biomol. NMR Assign. 9, 281-284 (2015).
PubMed: 25487676

Assembly members:

Assembly members:
HuR_RRM1, polymer, 101 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: RP1B

Data sets:
Data typeCount
13C chemical shifts412
15N chemical shifts106
1H chemical shifts666

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 101 residues - Formula weight is not available

Residues Gly-1 and His0 represent a cloning artifact and are derived from the TEV protease clevage site.

1   GLYHISMETSERASNGLYTYRGLUASPHIS
2   METALAGLUASPCYSARGGLYASPILEGLY
3   ARGTHRASNLEUILEVALASNTYRLEUPRO
4   GLNASNMETTHRGLNASPGLULEUARGSER
5   LEUPHESERSERILEGLYGLUVALGLUSER
6   ALALYSLEUILEARGASPLYSVALALAGLY
7   HISSERLEUGLYTYRGLYPHEVALASNTYR
8   VALTHRALALYSASPALAGLUARGALAILE
9   ASNTHRLEUASNGLYLEUARGLEUGLNSER
10   LYSTHRILELYSVALSERTYRALAARGPRO
11   SER

Samples:

sample_1: HuR_RRM1, [U-100% 15N], 1.5 mM; sodium phosphate 30 mM; sodium chloride 100 mM; DTT 10 mM; H2O 90%; D2O 10%

sample_2: HuR_RRM1, [U-100% 13C; U-100% 15N], 1.5 mM; sodium phosphate 30 mM; sodium chloride 100 mM; DTT 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D (H)CC(CO)NHsample_2isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

CARA v1.8.4, Prof. Kurt Wuttrich's group, ETH - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 800 MHz

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