BMRB Entry 17240
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17240
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Title: INFLUENZA HEMEGGLUTININ FUSION PEPTIDE MUTANT G13A PubMed: 20826788
Deposition date: 2010-10-05 Original release date: 2010-10-19
Authors: Lai, Alex; Tamm, Lukas
Citation: Lai, Alex; Tamm, Lukas. "Shallow Boomerang-shaped Influenza Hemagglutinin G13A Mutant Structure Promotes Leaky Membrane Fusion." J. Biol. Chem. 285, 37467-37475 (2010).
Assembly members:
Influenza_HA_fusion_peptide_G13A, polymer, 27 residues, Formula weight is not available
Natural source: Common Name: Influenza A virus Taxonomy ID: 11320 Superkingdom: virus Kingdom: not available Genus/species: Influenzavirus A not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Influenza_HA_fusion_peptide_G13A: GLFGAIAGFIENAWEGMIDG
GCGKKKK
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 117 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Influenza HA fusion peptide(G13A) | 1 |
Entities:
Entity 1, Influenza HA fusion peptide(G13A) 27 residues - Formula weight is not available
1 | GLY | LEU | PHE | GLY | ALA | ILE | ALA | GLY | PHE | ILE | ||||
2 | GLU | ASN | ALA | TRP | GLU | GLY | MET | ILE | ASP | GLY | ||||
3 | GLY | CYS | GLY | LYS | LYS | LYS | LYS |
Samples:
FP_N15: Influenza HA fusion peptide G13A, [U-15N], 1 mM; DPC, [U-2H], 200 mM; acetic acid, [U-2H], 20 mM; DTT 5 mM; H2O 95%; D2O 5%
FP: Influenza HA fusion peptide G13A, [U-15N], 2 mM; DPC, [U-2H], 200 mM; acetic acid, [U-2H], 20 mM; DTT 5 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 5; pressure: 1 atm; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H TOCSY | FP | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | FP | isotropic | sample_conditions_1 |
3D HNHA | FP_N15 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | FP_N15 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment, data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
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