BMRB Entry 26527
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26527
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Title: WHB PubMed: 25825779
Deposition date: 2015-03-02 Original release date: 2015-06-17
Authors: Brown, Nicholus; Grace, Christy
Citation: Brown, Nicholas; VanderLinden, Ryan; Watson, Edmond; Qiao, Renping; Grace, Christy; Yamaguchi, Masaya; Weissmann, Florian; Frye, Jeremiah; Dube, Prakash; Cho, Shein; Actis, Marcelo; Rodrigues, Patrick; Fujii, Naoaki; Peters, Jan-Michael; Stark, Holger; Schulman, Brenda. "RING E3 mechanism for ubiquitin ligation to a disordered substrate visualized for human anaphase-promoting complex" Proc. Natl. Acad. Sci. U. S. A. 17, 5272-5279 (2015).
Assembly members:
Molecule_1, polymer, 90 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Molecule_1: GSESDSGMASQADQKEEELL
LFWTYIQAMLTNLESLSLDR
IYNMLRMFVVTGPALAEIDL
QELQGYLQKKVRDQQLVYSA
GVYRLPKNCS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 230 |
15N chemical shifts | 85 |
1H chemical shifts | 85 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | molecule_1 | 1 |
Entities:
Entity 1, molecule_1 90 residues - Formula weight is not available
1 | GLY | SER | GLU | SER | ASP | SER | GLY | MET | ALA | SER | |
2 | GLN | ALA | ASP | GLN | LYS | GLU | GLU | GLU | LEU | LEU | |
3 | LEU | PHE | TRP | THR | TYR | ILE | GLN | ALA | MET | LEU | |
4 | THR | ASN | LEU | GLU | SER | LEU | SER | LEU | ASP | ARG | |
5 | ILE | TYR | ASN | MET | LEU | ARG | MET | PHE | VAL | VAL | |
6 | THR | GLY | PRO | ALA | LEU | ALA | GLU | ILE | ASP | LEU | |
7 | GLN | GLU | LEU | GLN | GLY | TYR | LEU | GLN | LYS | LYS | |
8 | VAL | ARG | ASP | GLN | GLN | LEU | VAL | TYR | SER | ALA | |
9 | GLY | VAL | TYR | ARG | LEU | PRO | LYS | ASN | CYS | SER |
Samples:
sample_1: Molecule_1, [U-100% 13C; U-100% 15N], 0.5 mM; DTT 0.01 mM; sodium chloride 0.1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment, 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