BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 12032

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR12032

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Title: Solution NMR structure of the W187R mutant of 1918 NS1 effector domain   PubMed: 31420169

Deposition date: 2019-01-31 Original release date: 2019-09-10

Authors: Shen, Qingliang; Cho, Jae-Hyun

Citation: Shen, Qingliang; Cho, Jae-Hyun. "The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus."  Biochem. Biophys. Res. Commun. 518, 178-182 (2019).

Assembly members:
NS1_effector_domain, polymer, 119 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
NS1_effector_domain: SRYLTDMTLEEMSRDWFMLM PKQKVAGSLCIRMDQAIMDK NIILKANFSVIFDRLETLIL LRAFTEEGAIVGEISPLPSL PGHTDEDVKNAVGVLIGGLE RNDNTVRVSETLQRFAWRS

Data sets:
Data typeCount
13C chemical shifts482
15N chemical shifts120
1H chemical shifts750

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NS1 effector domain1

Entities:

Entity 1, NS1 effector domain 119 residues - Formula weight is not available

1   SERARGTYRLEUTHRASPMETTHRLEUGLU
2   GLUMETSERARGASPTRPPHEMETLEUMET
3   PROLYSGLNLYSVALALAGLYSERLEUCYS
4   ILEARGMETASPGLNALAILEMETASPLYS
5   ASNILEILELEULYSALAASNPHESERVAL
6   ILEPHEASPARGLEUGLUTHRLEUILELEU
7   LEUARGALAPHETHRGLUGLUGLYALAILE
8   VALGLYGLUILESERPROLEUPROSERLEU
9   PROGLYHISTHRASPGLUASPVALLYSASN
10   ALAVALGLYVALLEUILEGLYGLYLEUGLU
11   ARGASNASPASNTHRVALARGVALSERGLU
12   THRLEUGLNARGPHEALATRPARGSER

Samples:

sample_1: NS1 effector domain, [U-98% 13C; U-98% 15N], 0.1 – 0.2 mM; sodium phosphate 20 mM; sodium chloride 80 mM; DTT 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: NS1 effector domain, [U-98% 13C; U-98% 15N], 0.1 – 0.15 mM; sodium phosphate 20 mM; sodium chloride 80 mM; DTT 1 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 80 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

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

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - structure solution

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

SPARKY vNMRFAM-Sparky 1.3, Goddard, National Magnetic Resonance Facility at Madison - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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