BMRB Entry 30261

Name: HnRNP A1 Alters the Conformation of a Conserved Enterovirus IRES Domain to Stimulate Viral Translation
Published: 2017-07-07

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PDB ID: 5v16
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30261
MolProbity Validation Chart

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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:

HnRNP A1 Alters the Conformation of a Conserved Enterovirus IRES Domain to Stimulate Viral Translation

Deposition date:

2017-03-01

Original release date:

2017-07-07

Authors:

Tolbert, M.; Morgan, C.; Tolbert, B.

Citation:

Citation: Tolbert, M.; Morgan, C.; Pollum, M.; Crespo-Hernandez, C.; Li, M.; Brewer, G.; Tolbert, B.. "HnRNP A1 Alters the Structure of a Conserved Enterovirus IRES Domain to Stimulate Viral Translation." J. Mol. Biol. 429, 2841-2858 (2017).
PubMed: 28625847

Assembly members:

Assembly members:
entity_1, polymer, 41 residues, 13140.855 Da.

Natural source:

Natural source: Common Name: Enterovirus A71 Taxonomy ID: 39054 Superkingdom: Viruses Kingdom: not available Genus/species: Enterovirus A71

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGAUCAAUAGCAGGUGUGGC ACACCAGUCAUACCUUGAUC C

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	131

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 41 residues - 13140.855 Da.

1

G

A

U

C

A

U

A

G

2

C

A

G

U

G

U

G

C

3

A

C

A

C

A

G

U

C

A

4

U

A

C

U

G

A

U

C

5

C

Samples:

sample_4: rNTP, [U-13C]-Gua, 300.0 uM

sample_1: rNTP, Selective Deuteration; EQUIMOLAR MIX:ATP, GTP, CTP, UTP, 180.0 ± 0.2 uM

sample_2: rNTP, Fully protonated, 300.0 ± 0.2 uM

sample_3: rNTP, Fully protonated, 100.0 uM

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HMQC	sample_4	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1

Software:

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

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

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 800 MHz