BMRB Entry 25779

Title:
Partial 1H, 13C and 15N backbone resonance assignments for the carboxy-terminal RNA recognition motif of Plasmodium falciparum Ser/Arg-rich protein 1
Deposition date:
2015-08-28
Original release date:
2018-12-21
Authors:
Ganguly, Akshay; Verma, Garima; Bhavesh, Neel Sarovar
Citation:

Citation: Ganguly, Akshay; Verma, Garima; Bhavesh, Neel Sarovar. "The N-terminal RNA Recognition Motif of PfSR1 Confers Semi-specificity for Pyrimidines during RNA Recognition"  J. Mol. Biol. ., .-. (2018).
PubMed: 30500338

Assembly members:

Assembly members:
RRM2, polymer, 84 residues, 9467.6 Da.

Natural source:

Natural source:   Common Name: malaria parasite   Taxonomy ID: 5833   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts131
15N chemical shifts71
1H chemical shifts71

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM21

Entities:

Entity 1, RRM2 84 residues - 9467.6 Da.

Residues G1 to M4 are from the pET28a vector.R107 to K186 are native amino acids of PfSR1-RRM2

1   GLYSERHISMETARGARGGLYARGTYRVAL
2   VALGLUVALTHRGLYLEUPROILESERGLY
3   SERTRPGLNASPLEULYSASPHISLEUARG
4   GLUALAGLYGLUCYSGLYHISALAASPVAL
5   PHELYSASPGLYTHRGLYGLUVALSERPHE
6   PHEASNLYSASPASPMETLEUGLUALAILE
7   ASPLYSPHEASNGLYSERILEPHEARGSER
8   HISGLUGLYGLULYSSERLYSILESERILE
9   ARGGLNLYSLYS

Samples:

PfSR1-RRM2: RRM2, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; sodium phosphate 25 mM; sodium chloride 100 mM; TCEP 3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 125 mM; pH: 5.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCPfSR1-RRM2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticPfSR1-RRM2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticPfSR1-RRM2isotropicsample_conditions_1
3D HNCACBPfSR1-RRM2isotropicsample_conditions_1
3D CBCA(CO)NHPfSR1-RRM2isotropicsample_conditions_1
3D C(CO)NHPfSR1-RRM2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance III 500 MHz
  • Bruker Avance III 700 MHz

Related Database Links:

NCBI XP_001351730.2

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