BMRB Entry 52245

Name: Backbone assignment of GLYCINE RICH RNA-BINDING PROTEIN 7 from Arabidopsis thaliana
Published: 2024-01-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52245

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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:

Backbone assignment of GLYCINE RICH RNA-BINDING PROTEIN 7 from Arabidopsis thaliana

Deposition date:

2023-12-17

Original release date:

2024-01-16

Authors:

Messini, Niki; Kachariya, Nitin; Sattler, Michael

Citation:

Citation: Lewinski, Martin; Steffen, Alexander; Kachariya, Nitin; Elgner, Mareike; Schmal, Christoph; Messini, Niki; Koster, Tino; Reichel, Marlene; Sattler, Michael; Zarnack, Kathi; Staiger, Dorothee. "Arabidopsis thaliana GLYCINE RICH RNA-BINDING PROTEIN 7 interaction with its iCLIP target LHCB1.1 correlates with changes in RNA stability and circadian oscillation" Plant J. 118, 203-224 (2024).
PubMed: 38124335

Assembly members:

Assembly members:
entity_1, polymer, 91 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MASGDVEYRCFVGGLAWATD DRALETAFAQYGDVIDSKII NDRETGRSRGFGFVTFKDEK AMKDAIEGMNGQDLDGRSIT VNEAQSRGSGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	258
15N chemical shifts	91
1H chemical shifts	91

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM	1

Entities:

Entity 1, RRM 91 residues - Formula weight is not available

1

MET

ALA

SER

GLY

ASP

VAL

GLU

TYR

ARG

CYS

2

PHE

VAL

GLY

LEU

ALA

TRP

ALA

THR

ASP

3

ASP

ARG

ALA

LEU

GLU

THR

ALA

PHE

ALA

GLN

4

TYR

GLY

ASP

VAL

ILE

ASP

SER

LYS

ILE

5

ASN

ASP

ARG

GLU

THR

GLY

ARG

SER

ARG

GLY

6

PHE

GLY

PHE

VAL

THR

PHE

LYS

ASP

GLU

LYS

7

ALA

MET

LYS

ASP

ALA

ILE

GLU

GLY

MET

ASN

8

GLY

GLN

ASP

LEU

ASP

GLY

ARG

SER

ILE

THR

9

VAL

ASN

GLU

ALA

GLN

SER

ARG

GLY

SER

GLY

10

GLY

Samples:

sample_1: Grp7 RRM, [U-99% 13C; U-99% 15N], 500 uM; Grp7 RRM, [U-100% 15N], 500 uM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNN	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5 pl 6 - collection, processing

NMRPipe - processing

CcpNMR v2.5 - chemical shift assignment, data analysis, peak picking

TALOS-N - chemical shift calculation

qMDD - processing

NMR spectrometers:

Bruker Avance 950 MHz
Bruker Avance 900 MHz
Bruker Avance 800 MHz
Bruker Avance 600 MHz
Bruker Avance 600 MHz
Bruker Avance 500 MHz