BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 51393

Title: drosophila pAbp RRM3   PubMed: 36688322

Deposition date: 2022-04-07 Original release date: 2023-07-04

Authors: Hollmann, Nele Merret; Simon, Bernd; Hennig, Janosch

Citation: Hollmann, Nele Merret; Jagtap, Pravin; Linse, Johanna-Barbara; Ullmann, Philip; Payr, Marco; Murciano, Brice; Simon, Bernd; Hub, Jochen; Hennig, Janosch. "Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein"  Nucleic Acids Res. 51, 1895-1913 (2023).

Assembly members:
entity_1, polymer, 88 residues, Formula weight is not available

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-11

Entity Sequences (FASTA):
entity_1: GEKAKLFTNVYVKNFTEDFD DEKLKEFFEPYGKITSYKVM SKEDGKSKGFGFVAFETTEA AEAAVQALNGKDMGEGKSLY VARAQKKA

Data sets:
Data typeCount
13C chemical shifts167
15N chemical shifts86
1H chemical shifts86

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1drosophila pAbp RRM31

Entities:

Entity 1, drosophila pAbp RRM3 88 residues - Formula weight is not available

1   GLYGLULYSALALYSLEUPHETHRASNVAL
2   TYRVALLYSASNPHETHRGLUASPPHEASP
3   ASPGLULYSLEULYSGLUPHEPHEGLUPRO
4   TYRGLYLYSILETHRSERTYRLYSVALMET
5   SERLYSGLUASPGLYLYSSERLYSGLYPHE
6   GLYPHEVALALAPHEGLUTHRTHRGLUALA
7   ALAGLUALAALAVALGLNALALEUASNGLY
8   LYSASPMETGLYGLUGLYLYSSERLEUTYR
9   VALALAARGALAGLNLYSLYSALA

Samples:

sample_1: pAbp RRM3, [U-99% 13C; U-99% 15N], 0.3 mM; sodium azide 0.01%; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 1 mM

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5pl7 - collection

NMRPipe - processing

CARA - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Related Database Links:

UNP P21187

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