BMRB Entry 27671

Name: Amide chemical shifts of human HuR RRM3
Published: 2018-11-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27671

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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:

Amide chemical shifts of human HuR RRM3

Deposition date:

2018-10-31

Original release date:

2018-11-14

Authors:

Pabis, Marta; Popowicz, Grzegorz; Schlundt, Andreas; Sattler, Michael

Citation:

Citation: Pabis, Marta; Popowicz, Grzegorz; Stehle, Ralf; Fernandez-Ramos, David; Asami, Sam; Warner, Lisa; Garcia-Maurino, Sofia; Schlundt, Andreas; Martinez-Chantar, Maria; Diaz-Moreno, Irene; Sattler, Michael. "HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs." Nucleic Acids Res. 47, 1011-1029 (2019).
PubMed: 30418581

Assembly members:

Assembly members:
HuR_RRM3, polymer, 87 residues, 9691.17 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET GST-1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HuR_RRM3: GAMGWCIFIYNLGQDADEGI LWQMFGPFGAVTNVKVIRDF NTNKCKGFGFVTMTNYEEAA MAIASLNGYRLGDKILQVSF KTNKSHK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	70
1H chemical shifts	69

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HuR RRM3	1

Entities:

Entity 1, HuR RRM3 87 residues - 9691.17 Da.

GAM is from cloning

1

GLY

ALA

MET

GLY

TRP

CYS

ILE

PHE

ILE

TYR

2

ASN

LEU

GLY

GLN

ASP

ALA

ASP

GLU

GLY

ILE

3

LEU

TRP

GLN

MET

PHE

GLY

PRO

PHE

GLY

ALA

4

VAL

THR

ASN

VAL

LYS

VAL

ILE

ARG

ASP

PHE

5

ASN

THR

ASN

LYS

CYS

LYS

GLY

PHE

GLY

PHE

6

VAL

THR

MET

THR

ASN

TYR

GLU

ALA

7

MET

ALA

ILE

ALA

SER

LEU

ASN

GLY

TYR

ARG

8

LEU

GLY

ASP

LYS

ILE

LEU

GLN

VAL

SER

PHE

9

LYS

THR

ASN

LYS

SER

HIS

LYS

Samples:

sample_1: HuR RRM3, [U-13C; U-15N], 120 uM; sodium phosphate 20 mM; sodium chloride 200 mM; DTT 5 mM; EDTA 1 mM

sample_2: HuR RRM3, [U-15N; U-2H], 120 uM; sodium phosphate 20 mM; sodium chloride 200 mM; DTT 5 mM; EDTA 1 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CCPNMR_Analysis v2.4, CCPN - chemical shift assignment

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

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

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