BMRB Entry 25793

Name: Solution Structure of the RNA-Binding domain of non-structural protein 1 from the 1918 H1N1 influenza virus
Published: 2015-09-28

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PDB ID: 2n74
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25793
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of the RNA-Binding domain of non-structural protein 1 from the 1918 H1N1 influenza virus PubMed: 26365801

Deposition date: 2015-09-03 Original release date: 2015-09-28

Authors: Jureka, Alexander; Kleinpeter, Alexander; Cornilescu, Gabriel; Cornilescu, Claudia; Schwieters, Charles; Petit, Chad

Citation: Jureka, Alexander; Kleinpeter, Alexander; Cornilescu, Gabriel; Cornilescu, Claudia; Schwieters, Charles; Petit, Chad. "Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I" Structure 23, 2001-2010 (2015).

Assembly members:
Influenza_NS1_RNA_Binding_Domain, polymer, 73 residues, 16801.115 Da.

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
Influenza_NS1_RNA_Binding_Domain: MDSNTVSSFQVDCFLWHVRK RFADQELGDAPFLDRLRRDQ KSLRGRGSTLGLDIETATRA GKQIVERILKEES

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	311
15N chemical shifts	71
1H chemical shifts	458

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 73 residues - 16801.115 Da.

1

MET

ASP

SER

ASN

THR

VAL

SER

PHE

GLN

2

VAL

ASP

CYS

PHE

LEU

TRP

HIS

VAL

ARG

LYS

3

ARG

PHE

ALA

ASP

GLN

GLU

LEU

GLY

ASP

ALA

4

PRO

PHE

LEU

ASP

ARG

LEU

ARG

ASP

GLN

5

LYS

SER

LEU

ARG

GLY

ARG

GLY

SER

THR

LEU

6

GLY

LEU

ASP

ILE

GLU

THR

ALA

THR

ARG

ALA

7

GLY

LYS

GLN

ILE

VAL

GLU

ARG

ILE

LEU

LYS

8

GLU

SER

Samples:

sample_1: Influenza NS1 RNA Binding Domain, [U-13C; U-15N], 1.0 mM; Ammonium Acetate pH 6.0 300 mM; EDTA 2.2 mM; sodium azide 0.1%; H2O 95%; D2O 5%

sample_2: Influenza NS1 RNA Binding Domain, [U-15N], 1 mM; Ammonium Acetate pH 6.0 300 mM; EDTA 2.0 mM; sodium azide 0.1%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 300 mM; pH: 6; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

TALOS, Cornilescu, Delaglio and Bax - refinement

NMR spectrometers:

Bruker Avance 850 MHz
Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts