BMRB Entry 11149
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11149
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Title: Structural study of the UBA domain of p62 and its interaction with ubiquitin
Deposition date: 2010-04-13 Original release date: 2012-08-02
Authors: Isogai, Shin; Tochio, Hidehito; Tenno, Takeshi; Morimoto, Daichi
Citation: Isogai, Shin; Tenno, Takeshi; Morimoto, Daichi; Tochio, Hidehito. "Structural study of the UBA domain of p62 and its interaction with ubiquitin" . ., .-..
Assembly members:
p62 UBA domain, polymer, 53 residues, 5817.546 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
p62 UBA domain: GPLGSEADPRLIESLSQMLS
MGFSDEGGWLTRLLQTKNYD
IGAALDTIQYSKH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 219 |
15N chemical shifts | 51 |
1H chemical shifts | 356 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | p62 UBA domain | 1 |
Entities:
Entity 1, p62 UBA domain 53 residues - 5817.546 Da.
1 | GLY | PRO | LEU | GLY | SER | GLU | ALA | ASP | PRO | ARG | ||||
2 | LEU | ILE | GLU | SER | LEU | SER | GLN | MET | LEU | SER | ||||
3 | MET | GLY | PHE | SER | ASP | GLU | GLY | GLY | TRP | LEU | ||||
4 | THR | ARG | LEU | LEU | GLN | THR | LYS | ASN | TYR | ASP | ||||
5 | ILE | GLY | ALA | ALA | LEU | ASP | THR | ILE | GLN | TYR | ||||
6 | SER | LYS | HIS |
Samples:
sample_1: p62 UBA domain, [U-95% 13C; U-95% 15N], 400 uM; ubiquitin 2.4 mM; EDTA 1 mM; potassium phosphate 20 mM; potassium chloride 5 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 0.025 M; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.113, Goddard - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
BMRB | 11443 15591 15592 |
PDB | |
DBJ | BAC26183 |
GB | AAH06019 AKI70216 EDL33719 EHH27114 EHH54825 |
REF | NP_001277698 XP_006246276 XP_006246277 XP_008273207 XP_008987787 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts