BMRB Entry 26922

Name: First RRM domain of MEC-8
Published: 2017-04-26

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26922

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MEC-8_RRM1: GAMASQVRTLFVSGLPMDAK PRELYLLFRGARGYEGALLK MTSKNGKPTSPVGFVTFLSQ QDAQDARKMLQGVRFDPEAA QVLRLELAKSNTKVARPKQS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	214
15N chemical shifts	100
1H chemical shifts	180

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MEC-8 RRM1, chain 1	1
2	MEC-8 RRM1, chain 2	1

Entities:

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

GAMA- at N-terminus remaining after TEV cleavage

1	GLY	ALA	MET	ALA	SER	GLN	VAL	ARG	THR	LEU
2	PHE	VAL	SER	GLY	LEU	PRO	MET	ASP	ALA	LYS
3	PRO	ARG	GLU	LEU	TYR	LEU	LEU	PHE	ARG	GLY
4	ALA	ARG	GLY	TYR	GLU	GLY	ALA	LEU	LEU	LYS
5	MET	THR	SER	LYS	ASN	GLY	LYS	PRO	THR	SER
6	PRO	VAL	GLY	PHE	VAL	THR	PHE	LEU	SER	GLN
7	GLN	ASP	ALA	GLN	ASP	ALA	ARG	LYS	MET	LEU
8	GLN	GLY	VAL	ARG	PHE	ASP	PRO	GLU	ALA	ALA
9	GLN	VAL	LEU	ARG	LEU	GLU	LEU	ALA	LYS	SER
10	ASN	THR	LYS	VAL	ALA	ARG	PRO	LYS	GLN	SER

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_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

UNP	G5ECJ4
AlphaFold	G5ECJ4

1	GLY	ALA	MET	ALA	SER	GLN	VAL	ARG	THR	LEU
2	PHE	VAL	SER	GLY	LEU	PRO	MET	ASP	ALA	LYS
3	PRO	ARG	GLU	LEU	TYR	LEU	LEU	PHE	ARG	GLY
4	ALA	ARG	GLY	TYR	GLU	GLY	ALA	LEU	LEU	LYS
5	MET	THR	SER	LYS	ASN	GLY	LYS	PRO	THR	SER
6	PRO	VAL	GLY	PHE	VAL	THR	PHE	LEU	SER	GLN
7	GLN	ASP	ALA	GLN	ASP	ALA	ARG	LYS	MET	LEU
8	GLN	GLY	VAL	ARG	PHE	ASP	PRO	GLU	ALA	ALA
9	GLN	VAL	LEU	ARG	LEU	GLU	LEU	ALA	LYS	SER
10	ASN	THR	LYS	VAL	ALA	ARG	PRO	LYS	GLN	SER

1	GLY	ALA	MET	ALA	SER	GLN	VAL	ARG	THR	LEU
2	PHE	VAL	SER	GLY	LEU	PRO	MET	ASP	ALA	LYS
3	PRO	ARG	GLU	LEU	TYR	LEU	LEU	PHE	ARG	GLY
4	ALA	ARG	GLY	TYR	GLU	GLY	ALA	LEU	LEU	LYS
5	MET	THR	SER	LYS	ASN	GLY	LYS	PRO	THR	SER
6	PRO	VAL	GLY	PHE	VAL	THR	PHE	LEU	SER	GLN
7	GLN	ASP	ALA	GLN	ASP	ALA	ARG	LYS	MET	LEU
8	GLN	GLY	VAL	ARG	PHE	ASP	PRO	GLU	ALA	ALA
9	GLN	VAL	LEU	ARG	LEU	GLU	LEU	ALA	LYS	SER
10	ASN	THR	LYS	VAL	ALA	ARG	PRO	LYS	GLN	SER