BMRB Entry 50804

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50804

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Title:
1H, 13C and 15N chemical shift assignments of RNA binding protein RBM3
Deposition date:
2021-03-07
Original release date:
2021-12-13
Authors:
Boral, Soumendu; Roy, Sayantani; Basak, Aditya; Maiti, Snigdha; De, Soumya
Citation:

Citation: Roy, Sayantani; Boral, Soumendu; Maiti, Snigdha; Kushwaha, Tushar; Basak, Aditya; Lee, Woonghee; Basak, Amit; Gholap, Shivajirao; Inampudi, Krishna; De, Soumya. "Structural and dynamic studies of the human RNA binding protein RBM3 reveals the molecular basis of its oligomerization and RNA recognition"  FEBS J. 289, 2847-2864 (2021).
PubMed: 34837346

Assembly members:

Assembly members:
entity_1, polymer, 84 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-28(a)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSSEEGKLFVGGLNFNTDEQ ALEDHFSSFGPISEVVVVKD RETQRSRGFGFITFTNPEHA SVAMRAMNGESLDGRQIRVD HAGK

Data sets:
Data typeCount
13C chemical shifts322
15N chemical shifts90
1H chemical shifts522

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RNA Recognition Motif1

Entities:

Entity 1, RNA Recognition Motif 84 residues - Formula weight is not available

1   METSERSERGLUGLUGLYLYSLEUPHEVAL
2   GLYGLYLEUASNPHEASNTHRASPGLUGLN
3   ALALEUGLUASPHISPHESERSERPHEGLY
4   PROILESERGLUVALVALVALVALLYSASP
5   ARGGLUTHRGLNARGSERARGGLYPHEGLY
6   PHEILETHRPHETHRASNPROGLUHISALA
7   SERVALALAMETARGALAMETASNGLYGLU
8   SERLEUASPGLYARGGLNILEARGVALASP
9   HISALAGLYLYS

Samples:

sample_1: RNA Recognition Motif, [U-100% 15N], 1.0 mM; RNA Recognition Motif, [U-100% 13C; U-100% 15N], 0.6 mM; RNA Recognition Motif, [U-10% 13C; U-100% 15N], 0.7 mM; sodium phosphate buffer 10 mM; NaCl 200 mM

sample_conditions_1: pH: 6.5; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

Related Database Links:

UNP P98179
AlphaFold P98179

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