BMRB Entry 52173

Name: NMR assignment of the Y5pCMF variant of human HuR RRM1 protein
Published: 2024-06-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52173

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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:

NMR assignment of the Y5pCMF variant of human HuR RRM1 protein

Deposition date:

2023-10-15

Original release date:

2024-06-19

Authors:

Banos-Jaime, Blanca; Perez-Mejias, Gonzalo; Corrales-Guerrero, Laura; De la Rosa, Miguel Angel; Diaz-Moreno, Irene

Citation:

Citation: Banos-Jaime, Blanca; Corrales-Guerrero, Laura; Perez-Mejias, Gonzalo; Rejano-Gordillo, Claudia Maria; Velazquez-Campoy, Adrian; Martinez-Cruz, Luis Alfonso; Martinez-Chantar, Maria Luz; De la Rosa, Miguel A.; Diaz-Moreno, Irene. "Phosphorylation at the disordered N-end makes HuR accumulate and dimerize in the cytoplasm" Nucleic Acids Res. 52, 8552-8565 (2024).
PubMed: 38966993

Assembly members:

Assembly members:
entity_1, polymer, 115 residues, 12850.445 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: pVC1 (from pGEX-4T-2)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHLVPRGSPGIPSNG XEDHMAEDCRGDIGRTNLIV NYLPQNMTQDELRSLFSSIG EVESAKLIRDKVAGHSLGYG FVNYVTAKDAERAINTLNGL RLQSKTIKVSYARPS

Data sets:

assigned_chemical_shifts

Data type	Count
13C chemical shifts	181
15N chemical shifts	114
1H chemical shifts	460

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HuR RRM1	1

Entities:

Entity 1, HuR RRM1 115 residues - 12850.445 Da.

Residues from 1 to 17 represent a non-native affinity tag. HuR protein sequence starts at residue 18, Ser2. Tyr5 is referred to HuR protein sequence.

1

MET

HIS

LEU

VAL

PRO

2

ARG

GLY

SER

PRO

GLY

ILE

PRO

SER

ASN

GLY

3

pCMF

GLU

ASP

HIS

MET

ALA

GLU

ASP

CYS

ARG

4

GLY

ASP

ILE

GLY

ARG

THR

ASN

LEU

ILE

VAL

5

ASN

TYR

LEU

PRO

GLN

ASN

MET

THR

GLN

ASP

6

GLU

LEU

ARG

SER

LEU

PHE

SER

ILE

GLY

7

GLU

VAL

GLU

SER

ALA

LYS

LEU

ILE

ARG

ASP

8

LYS

VAL

ALA

GLY

HIS

SER

LEU

GLY

TYR

GLY

9

PHE

VAL

ASN

TYR

VAL

THR

ALA

LYS

ASP

ALA

10

GLU

ARG

ALA

ILE

ASN

THR

LEU

ASN

GLY

LEU

11

ARG

LEU

GLN

SER

LYS

THR

ILE

LYS

VAL

SER

12

TYR

ALA

ARG

PRO

SER

Samples:

sample_1: HuR RRM1 Y5pCMF, [U-100% 13C; U-100% 15N], 690 uM; Sodium citrate 20 mM; sodium chloride 100 mM; TCEP 5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 278 K

sample_conditions_3: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HISQC	sample_1	isotropic	sample_conditions_2
2D (H2C)N(CC)H-TOCSY	sample_1	isotropic	sample_conditions_3
2D H2CN	sample_1	isotropic	sample_conditions_2
2D H2CN	sample_1	isotropic	sample_conditions_3

Software:

NMRFAM-SPARKY v1.470 - chemical shift assignment, peak picking

TOPSPIN v4.0.7 - collection

NMRPipe v10.9 - processing

NMR spectrometers:

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