BMRB Entry 16206

Name: THE RRM DOMAIN IN GW182 PROTEINS CONTRIBUTES TO MIRNA-MEDIATED GENE SILENCING
Published: 2009-03-30

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16206

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

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Title:

THE RRM DOMAIN IN GW182 PROTEINS CONTRIBUTES TO MIRNA-MEDIATED GENE SILENCING

Deposition date:

2009-03-09

Original release date:

2009-03-30

Authors:

Eulalio, A.; Tritschler, F.; Buettner, R.; Weichenrieder, O.; Izaurralde, E.; Truffault, V.

Citation:

Citation: Eulalio, Ana; Tritschler, Felix; Buettner, Regina; Weichenrieder, Oliver; Izaurralde, Elisa; Truffault, Vincent. "The RRM Domain in GW182 Proteins Contributes to miRNA-mediated gene silencing" Nucleic Acids Res. 37, 2974-2983 (2009).
PubMed: 19295135

Assembly members:

Assembly members:
RRM_DOMAIN_OF_GW182, polymer, 89 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI Vector: PETM60

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RRM_DOMAIN_OF_GW182: GAMAWGSSWLLLKNLTAQID GPTLRTLCMQHGPLVSFHPY LNQGIALCKYTTREEANKAQ MALNNCVLANTTIFAESPSE NEVQSIMQH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	336
15N chemical shifts	94
1H chemical shifts	600

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM DOMAIN OF GW182	1

Entities:

Entity 1, RRM DOMAIN OF GW182 89 residues - Formula weight is not available

1

GLY

ALA

MET

ALA

TRP

GLY

SER

TRP

LEU

2

LEU

LYS

ASN

LEU

THR

ALA

GLN

ILE

ASP

3

GLY

PRO

THR

LEU

ARG

THR

LEU

CYS

MET

GLN

4

HIS

GLY

PRO

LEU

VAL

SER

PHE

HIS

PRO

TYR

5

LEU

ASN

GLN

GLY

ILE

ALA

LEU

CYS

LYS

TYR

6

THR

ARG

GLU

ALA

ASN

LYS

ALA

GLN

7

MET

ALA

LEU

ASN

CYS

VAL

LEU

ALA

ASN

8

THR

ILE

PHE

ALA

GLU

SER

PRO

SER

GLU

9

ASN

GLU

VAL

GLN

SER

ILE

MET

GLN

HIS

Samples:

sample_1: RRM DOMAIN OF GW182, [U-100% 13C; U-100% 15N], 1 mM

sample_2: RRM DOMAIN OF GW182, [U-100% 15N], 1 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1.0 ATM; temperature: 298.0 K

Experiments:

Name	Sample	Sample state	Sample conditions
CBCACONH	sample_1	isotropic	sample_conditions_1
CCCONH	sample_1	isotropic	sample_conditions_1
CCHCOSY	sample_1	isotropic	sample_conditions_1
CCHNOESY	sample_1	isotropic	sample_conditions_1
CCHTOCSY	sample_1	isotropic	sample_conditions_1
CHSQC	sample_1	isotropic	sample_conditions_1
CNHNOESY	sample_1	isotropic	sample_conditions_1
HBHACONH	sample_1	isotropic	sample_conditions_1
HCHNOESY	sample_1	isotropic	sample_conditions_1
HNCA	sample_1	isotropic	sample_conditions_1
HNCACO	sample_1	isotropic	sample_conditions_1
HNCACB	sample_1	isotropic	sample_conditions_1
HNCO	sample_1	isotropic	sample_conditions_1
HNHA	sample_1	isotropic	sample_conditions_1
HNHB	sample_1	isotropic	sample_conditions_1
HNHNOESY	sample_1	isotropic	sample_conditions_1
NHSQC	sample_1	isotropic	sample_conditions_1
NNHNOESY	sample_1	isotropic	sample_conditions_1
NOESYNON	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH v2.9.4A, BRUNGER - refinement

SPARKY, Goddard - structure solution

NMR spectrometers:

BRUKER AVANCE III 800 MHz