BMRB Entry 17638
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17638
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Title: NMR Structure of the Complete Internal Fusion Loop from Ebolavirus GP2 at pH 5.5 PubMed: 21690393
Deposition date: 2011-05-12 Original release date: 2011-08-03
Authors: Gregory, S.; Harada, E.; Liang, B.; Tamm, L.
Citation: Gregory, Sonia; Harada, Erisa; Liang, Binyong; Delos, Sue; White, Judith; Tamm, Lukas. "Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2." Proc. Natl. Acad. Sci. U. S. A. ., .-. (2011).
Assembly members:
Ebolavirus_Fusion_Loop_pH_5.5, polymer, 54 residues, 5947.741 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):
Ebolavirus_Fusion_Loop_pH_5.5: AQPKCNPNLHYWTTQDEGAA
IGLAWIPYFGPAAEGIYIEG
LMHNQDGLICGLRQ
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 137 |
15N chemical shifts | 48 |
1H chemical shifts | 338 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Ebolavirus Fusion Loop pH 5.5 | 1 |
Entities:
Entity 1, Ebolavirus Fusion Loop pH 5.5 54 residues - 5947.741 Da.
1 | ALA | GLN | PRO | LYS | CYS | ASN | PRO | ASN | LEU | HIS | ||||
2 | TYR | TRP | THR | THR | GLN | ASP | GLU | GLY | ALA | ALA | ||||
3 | ILE | GLY | LEU | ALA | TRP | ILE | PRO | TYR | PHE | GLY | ||||
4 | PRO | ALA | ALA | GLU | GLY | ILE | TYR | ILE | GLU | GLY | ||||
5 | LEU | MET | HIS | ASN | GLN | ASP | GLY | LEU | ILE | CYS | ||||
6 | GLY | LEU | ARG | GLN |
Samples:
sample_1: Ebolavirus Fusion Loop pH 5.5, [U-13C; U-15N], 0.5-1 mM; H2O 90%; D2O 10%; sodium phosphate 30 mM; sodium chloride 50 mM
sample_2: Ebolavirus Fusion Loop pH 5.5, [U-15N], 0.5-1 mM; H2O 90%; D2O 10%; sodium phosphate 30 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 273 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | 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 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker DRX 600 MHz
- Varian NMRS 600 MHz
Related Database Links:
BMRB | 17639 19383 |
PDB | |
GB | AAA96744 AAB37095 AAB81004 AAC54887 AAC57989 |
REF | NP_066246 |
SP | O11457 P87666 Q05320 |
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