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Biological Magnetic Resonance Data Bank


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BMRB Entry 25650

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25650
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Title: Solution structure of RNA recognition motif-1 of Plasmodium falciparum serine/arginine-rich protein 1.   PubMed: 30500338

Deposition date: 2015-06-05 Original release date: 2016-07-18

Authors: Ganguly, Akshay Kumar; Verma, Garima; Bhavesh, Neel Sarovar

Citation: Ganguly, Akshay Kumar; 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).

Assembly members:
PfSR1-RRM1, polymer, 89 residues, 9997.284 Da.

Natural source:   Common Name: malaria parasite P. faciparum   Taxonomy ID: 5833   Superkingdom: Eukaryota   Kingdom: Chromalveolata   Genus/species: Plasmodium falciparum

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

Entity Sequences (FASTA):
PfSR1-RRM1: GSHMVIRESVSRIYVGNLPS HVSSRDVENEFRKYGNILKC DVKKTVSGAAFAFIEFEDAR DAADAIKEKDGCDFEGNKLR VEVPFNARE

Data sets:
Data typeCount
13C chemical shifts356
15N chemical shifts84
1H chemical shifts491

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1RNA recognition motif-1 of serine/arginine-rich protein 11

Entities:

Entity 1, RNA recognition motif-1 of serine/arginine-rich protein 1 89 residues - 9997.284 Da.

Residues G, S and H at the amino terminus are derived from the vector pET28a and have been numbered as -2, -1 and 0, respectively.

1   GLYSERHISMETVALILEARGGLUSERVAL
2   SERARGILETYRVALGLYASNLEUPROSER
3   HISVALSERSERARGASPVALGLUASNGLU
4   PHEARGLYSTYRGLYASNILELEULYSCYS
5   ASPVALLYSLYSTHRVALSERGLYALAALA
6   PHEALAPHEILEGLUPHEGLUASPALAARG
7   ASPALAALAASPALAILELYSGLULYSASP
8   GLYCYSASPPHEGLUGLYASNLYSLEUARG
9   VALGLUVALPROPHEASNALAARGGLU

Samples:

sample_1: PfSR1-RRM1, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; sodium phosphate 25 mM; sodium chloride 100 mM; TCEP 3 mM; L-arginine 50 mM; L-glutamate 25 mM; D2O 10%; H2O 90%

sample_d2o: PfSR1-RRM1, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; sodium phosphate 25 mM; sodium chloride 100 mM; TCEP 3 mM; L-arginine 50 mM; L-glutamate 25 mM; D2O 100%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_d2oisotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

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

CYANA, Guntert, Mumenthaler and Wuthrich - peak picking, structure solution

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

Related Database Links:

NCBI XP_001351730.2

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts