BMRB Entry 51824

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51824

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Title:
1H, 13C, 15N backbone NMR resonance assignments for the N-terminal RNA recognition motif of the Sorghum Glycine-Rich RNA-Binding Protein(SbGRBP)
Deposition date:
2023-02-06
Original release date:
2024-11-19
Authors:
Singh, Harpreet; Paithankar, Harshad; Singh, Supreet; Singh, Prabhjeet; Kumar, Ashutosh; Mithu, Venus Singh
Citation:

Citation: Singh, Harpreet; Paithankar, Harshad; Poojari, Chetan; Kaur, Kirandeep; Singh, Supreet; Shobhawat, Rahul; Singh, Prabhjeet; Kumar, Ashutosh; Mithu, Venus Singh. "Structural insights to the RRM-domain of the glycine-rich RNA-binding protein from Sorghum bicolor and its role in cold stress tolerance in E. coli"  Int. J. Biol. Macromol. 282, 136668-136668 (2024).
PubMed: 39442831

Assembly members:

Assembly members:
entity_1, polymer, 131 residues, 13587 Da.

Natural source:

Natural source:   Common Name: Sorghum bicolor   Taxonomy ID: 4558   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Sorghum bicolor

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28a+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAAFNKLGSLLRHSALASGV AASSSPAVFNAARLMSTKLF VGGLSWGVDDMKLREAFSGF GDVTEARVITDRDTGKSRGF GFVNYTSSDAANAAISGMDG KEIDGRPVRVNIANDRPAGN APPPPPLRSGC

Data sets:
Data typeCount
13C chemical shifts282
15N chemical shifts101
1H chemical shifts101

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SbGRBP1

Entities:

Entity 1, SbGRBP 131 residues - 13587 Da.

Residues NAPPPPPLRSGC at the C terminal is part of the fusion tag of the protein.

1   METALAALAPHEASNLYSLEUGLYSERLEU
2   LEUARGHISSERALALEUALASERGLYVAL
3   ALAALASERSERSERPROALAVALPHEASN
4   ALAALAARGLEUMETSERTHRLYSLEUPHE
5   VALGLYGLYLEUSERTRPGLYVALASPASP
6   METLYSLEUARGGLUALAPHESERGLYPHE
7   GLYASPVALTHRGLUALAARGVALILETHR
8   ASPARGASPTHRGLYLYSSERARGGLYPHE
9   GLYPHEVALASNTYRTHRSERSERASPALA
10   ALAASNALAALAILESERGLYMETASPGLY
11   LYSGLUILEASPGLYARGPROVALARGVAL
12   ASNILEALAASNASPARGPROALAGLYASN
13   ALAPROPROPROPROPROLEUARGSERGLY
14   CYS

Samples:

sample_1: SbGRBP, [U-100% 13C; U-100% 15N], 1.2 mM; D2O, [U-100% 2H], 10%; DTT 1 mM; sodium chloride 300 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 300 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6 - collection, processing

CARA v1.9 - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 750 MHz
  • Bruker Avance 800 MHz
  • Bruker AVANCE III 950 MHz

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