Biological Magnetic Resonance Data Bank

A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18617

Title: Conformational ensemble for the G8A mutant of the influenza hemagglutinin fusion peptide   PubMed: 23169643

Authors: Lorieau, Justin; Louis, John; Schwieters, Charles; Bax, Ad

Citation: Lorieau, Justin; Louis, John; Schwieters, Charles; Bax, Ad. "pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR"  Proc. Natl. Acad. Sci. U. S. A. 109, 19994-19999 (2012).

Assembly members:
Hemagglutinin_Fusion_Peptide_G8A_mutant, polymer, 30 residues, 3165.648 Da.

Natural source:   Common Name: Influenza A virus   Taxonomy ID: 11320   Superkingdom: Viruses   Kingdom: not available   Genus/species: Influenzavirus A Influenza A virus

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

Entity Sequences (FASTA):
Hemagglutinin_Fusion_Peptide_G8A_mutant: GLFGAIAAFIEGGWTGMIDG WYGSGKKKKD

Data sets:
Data typeCount
13C chemical shifts23
15N chemical shifts21
1H chemical shifts51
heteronuclear NOE values21
H exchange rates21
T1 relaxation values42
T2 relaxation values42

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID
1Hemagglutinin_Fusion_Peptide_G8A_mutant, strand 11
2Hemagglutinin_Fusion_Peptide_G8A_mutant, strand 21
3Hemagglutinin_Fusion_Peptide_G8A_mutant, strand 31


Entity 1, Hemagglutinin_Fusion_Peptide_G8A_mutant, strand 1 30 residues - 3165.648 Da.



sample_1: Hemagglutinin Fusion Peptide G8A mutant, [U-100% 13C; U-100% 15N], 0.3 – 0.6 mM; TRIS 25 mM; DPC, [U-100% 2H], 130 – 160 mM; D2O 7%; H2O 93%

sample_conditions_1: ionic strength: 0 M; pH: 7.3; pressure: 1 atm; temperature: 305.0 K

sample_conditions_2: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 305.0 K


NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1


NMRPipe v7.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.113, Goddard - chemical shift assignment

X-PLOR NIH v2.31, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 750 MHz

Related Database Links:

GB AEL63841