BMRB Entry 34080

Name: hnRNP A1 RRM2 in complex with 5&#039;-UCAGUU-3&#039; RNA
Published: 2017-06-30

Click here to enlarge.

PDB ID: 5mpl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34080
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

hnRNP A1 RRM2 in complex with 5'-UCAGUU-3' RNA

Deposition date:

2016-12-16

Original release date:

2017-06-30

Authors:

Barraud, P.; Allain, F.

Citation:

Citation: Beusch, Irene; Barraud, Pierre; Moursy, Ahmed; Clery, Antoine; Allain, Frederic Hai-Trieu. "Tandem hnRNP A1 RNA recognition motifs act in concert to repress the splicing of survival motor neuron exon 7" Elife 6, e25736-e25736 (2017).
PubMed: 28650318

Assembly members:

Assembly members:
Heterogeneous nuclear ribonucleoprotein A1, polymer, 102 residues, 11630.084 Da.
RNA UCAGUU, polymer, 6 residues, 1853.133 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Heterogeneous nuclear ribonucleoprotein A1: SQRPGAHLTVKKIFVGGIKE DTEEHHLRDYFEQYGKIEVI EIMTDRGSGKKRGFAFVTFD DHDSVDKIVIQKYHTVNGHN CEVRKALSKQEMASASSSQR GR
RNA UCAGUU: UCAGUU

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	293
15N chemical shifts	92
1H chemical shifts	654

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 102 residues - 11630.084 Da.

1

SER

GLN

ARG

PRO

GLY

ALA

HIS

LEU

THR

VAL

2

LYS

ILE

PHE

VAL

GLY

ILE

LYS

GLU

3

ASP

THR

GLU

HIS

LEU

ARG

ASP

TYR

4

PHE

GLU

GLN

TYR

GLY

LYS

ILE

GLU

VAL

ILE

5

GLU

ILE

MET

THR

ASP

ARG

GLY

SER

GLY

LYS

6

LYS

ARG

GLY

PHE

ALA

PHE

VAL

THR

PHE

ASP

7

ASP

HIS

ASP

SER

VAL

ASP

LYS

ILE

VAL

ILE

8

GLN

LYS

TYR

HIS

THR

VAL

ASN

GLY

HIS

ASN

9

CYS

GLU

VAL

ARG

LYS

ALA

LEU

SER

LYS

GLN

10

GLU

MET

ALA

SER

ALA

SER

GLN

ARG

11

GLY

ARG

Entity 2, entity_2 6 residues - 1853.133 Da.

1

U

C

A

G

U

Samples:

sample_1: RNA UCAGUU 1.0 g/L; hnRNP A1 RRM2, [U-99% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_2: RNA UCAGUU 1.0 mM; hnRNP A1 RRM2, [U-99% 13C; U-99% 15N], 1.0 mM; H2O 90%; D2O 10%

sample_3: RNA UCAGUU 1.0 mM; hnRNP A1 RRM2, [U-99% 15N], 1.0 mM; D2O 100%

sample_4: RNA UCAGUU 1.0 mM; hnRNP A1 RRM2, [U-99% 13C; U-99% 15N], 1.0 mM; D2O 100%

sample_conditions_1: ionic strength: 10 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_4	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_4	isotropic	sample_conditions_1
3D HNCA	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 HCc(CO)NH TOCSY	sample_2	isotropic	sample_conditions_1
3D hCC(CO)NH TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
3D F1eF3f 13C-filtered/edited NOESY	sample_4	isotropic	sample_conditions_1
2D F1fF2f 13C-filtered NOESY	sample_4	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ProcheckNMR, Laskowski and MacArthur - data analysis

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker AvanceIII 500 MHz
Bruker AvanceIII 600 MHz
Bruker AvanceIII 750 MHz
Bruker AvanceIII 700 MHz
Bruker Avance 900 MHz

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