BMRB Entry 26922

Title:
First RRM domain of MEC-8
Deposition date:
2016-10-24
Original release date:
2017-04-26
Authors:
Soufari, Heddy; Mackereth, Cameron
Citation:

Citation: Soufari, Heddy; Mackereth, Cameron. "Conserved binding of GCAC motifs by MEC-8, couch potato and the RBPMS protein family"  RNA 23, 308-316 (2017).
PubMed: 28003515

Assembly members:

Assembly members:
MEC-8_RRM1, polymer, 100 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Caenorhabditis elegans   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-His1a

Data sets:
Data typeCount
13C chemical shifts214
15N chemical shifts100
1H chemical shifts180

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MEC-8 RRM1, chain 11
2MEC-8 RRM1, chain 21

Entities:

Entity 1, MEC-8 RRM1, chain 1 100 residues - Formula weight is not available

GAMA- at N-terminus remaining after TEV cleavage

1   GLYALAMETALASERGLNVALARGTHRLEU
2   PHEVALSERGLYLEUPROMETASPALALYS
3   PROARGGLULEUTYRLEULEUPHEARGGLY
4   ALAARGGLYTYRGLUGLYALALEULEULYS
5   METTHRSERLYSASNGLYLYSPROTHRSER
6   PROVALGLYPHEVALTHRPHELEUSERGLN
7   GLNASPALAGLNASPALAARGLYSMETLEU
8   GLNGLYVALARGPHEASPPROGLUALAALA
9   GLNVALLEUARGLEUGLULEUALALYSSER
10   ASNTHRLYSVALALAARGPROLYSGLNSER

Samples:

sample_1: MEC-8 RRM1, [U-99% 13C; U-99% 15N], 300 uM; TRIS 50 mM; sodium chloride 150 mM; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

UNP G5ECJ4
AlphaFold G5ECJ4

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