BMRB Entry 25793

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

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).
PubMed: 26365801

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-SUMO

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts311
15N chemical shifts71
1H chemical shifts458

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 73 residues - 16801.115 Da.

1   METASPSERASNTHRVALSERSERPHEGLN
2   VALASPCYSPHELEUTRPHISVALARGLYS
3   ARGPHEALAASPGLNGLULEUGLYASPALA
4   PROPHELEUASPARGLEUARGARGASPGLN
5   LYSSERLEUARGGLYARGGLYSERTHRLEU
6   GLYLEUASPILEGLUTHRALATHRARGALA
7   GLYLYSGLNILEVALGLUARGILELEULYS
8   GLUGLUSER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks