BMRB Entry 25244

Name: 1H, 15N and 13C resonance assignments of the RRM1 domain of the key post-transcriptional regulator HuR
Published: 2015-09-04

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25244

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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:

1H, 15N and 13C resonance assignments of the RRM1 domain of the key post-transcriptional regulator HuR

Deposition date:

2014-09-23

Original release date:

2015-09-04

Authors:

Mujo, Amanda; Lixa, Carolina; Anobom, Cristiane; Almeida, Fabio; Pinheiro, Anderson

Citation:

Citation: Mujo, Amanda; Lixa, Carolina; Carneiro, Letcia; Anobom, Cristiane; Almeida, Fabio; Pinheiro, Anderson. "1H, 15N and 13C resonance assignments of the RRM1 domain of the key post-transcriptional regulator HuR" Biomol. NMR Assign. 9, 281-284 (2015).
PubMed: 25487676

Assembly members:

Assembly members:
HuR_RRM1, polymer, 101 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: RP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HuR_RRM1: GHMSNGYEDHMAEDCRGDIG RTNLIVNYLPQNMTQDELRS LFSSIGEVESAKLIRDKVAG HSLGYGFVNYVTAKDAERAI NTLNGLRLQSKTIKVSYARP S

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	412
15N chemical shifts	106
1H chemical shifts	666

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 101 residues - Formula weight is not available

Residues Gly-1 and His0 represent a cloning artifact and are derived from the TEV protease clevage site.

1

GLY

HIS

MET

SER

ASN

GLY

TYR

GLU

ASP

HIS

2

MET

ALA

GLU

ASP

CYS

ARG

GLY

ASP

ILE

GLY

3

ARG

THR

ASN

LEU

ILE

VAL

ASN

TYR

LEU

PRO

4

GLN

ASN

MET

THR

GLN

ASP

GLU

LEU

ARG

SER

5

LEU

PHE

SER

ILE

GLY

GLU

VAL

GLU

SER

6

ALA

LYS

LEU

ILE

ARG

ASP

LYS

VAL

ALA

GLY

7

HIS

SER

LEU

GLY

TYR

GLY

PHE

VAL

ASN

TYR

8

VAL

THR

ALA

LYS

ASP

ALA

GLU

ARG

ALA

ILE

9

ASN

THR

LEU

ASN

GLY

LEU

ARG

LEU

GLN

SER

10

LYS

THR

ILE

LYS

VAL

SER

TYR

ALA

ARG

PRO

11

SER

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D (H)CC(CO)NH	sample_2	isotropic	sample_conditions_1
3D HC(C)H-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Download HSQC peak lists in one of the following formats:
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BMRB Entry 25244

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: