BMRB Entry 19494

Name: HuR RRM3 WT
Published: 2015-02-05

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19494

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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:

HuR RRM3 WT

Deposition date:

2013-09-16

Original release date:

2015-02-05

Authors:

Blanco, Francisco; Scheiba, Rafael; Ibanez de Opakua, Alain

Citation:

Citation: Scheiba, Rafael; Ibanez de Opakua, Alain; Diaz-Quintana, Antonio; Cruz-Gallardo, Isabel; Martinez-Cruz, Luis; Martinez-Chantar, Maria; Blanco, Francisco; Diaz-Moreno, Irene. "The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets" RNA Biol. 11, 1250-1261 (2014).
PubMed: 25584704

Assembly members:

Assembly members:
HUR_RRM3_polypeptide, polymer, 124 residues, Formula weight is not available

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 M11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HUR_RRM3_polypeptide: MKHHHHHHPMSDYDIPTTEI SGRENLYFQSGSEFPAETPS GWCIFIYNLGQDADEGILWQ MFGPFGAVTNVKVIRDFNTN KCKGFGFVTMTNYEEAAMAI ASLNGYRLGDKILQVSFKTN KSHK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	204
15N chemical shifts	109
1H chemical shifts	184

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HUR RRM3	1

Entities:

Entity 1, HUR RRM3 124 residues - Formula weight is not available

Residues 1-41 represent a non-native linker with an affinity tag

1

MET

LYS

HIS

PRO

MET

2

SER

ASP

TYR

ASP

ILE

PRO

THR

GLU

ILE

3

SER

GLY

ARG

GLU

ASN

LEU

TYR

PHE

GLN

SER

4

GLY

SER

GLU

PHE

PRO

ALA

GLU

THR

PRO

SER

5

GLY

TRP

CYS

ILE

PHE

ILE

TYR

ASN

LEU

GLY

6

GLN

ASP

ALA

ASP

GLU

GLY

ILE

LEU

TRP

GLN

7

MET

PHE

GLY

PRO

PHE

GLY

ALA

VAL

THR

ASN

8

VAL

LYS

VAL

ILE

ARG

ASP

PHE

ASN

THR

ASN

9

LYS

CYS

LYS

GLY

PHE

GLY

PHE

VAL

THR

MET

10

THR

ASN

TYR

GLU

ALA

MET

ALA

ILE

11

ALA

SER

LEU

ASN

GLY

TYR

ARG

LEU

GLY

ASP

12

LYS

ILE

LEU

GLN

VAL

SER

PHE

LYS

THR

ASN

13

LYS

SER

HIS

LYS

Samples:

sample_1: HUR RRM3 polypeptide, [U-99% 13C; U-99% 15N], 233 uM; DTT 3 mM; D2O 5%; sodium azide 0.02%; DSS 30 uM; sodium phosphate 10 mM

sample_conditions_1: pH: 7.3; 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-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)HA	sample_1	isotropic	sample_conditions_1
3D HN(CA)HA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - data analysis, peak picking

MARS, (MARS) Zweckstetter - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz