BMRB Entry 15111
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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/BMR15111
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Title: Solution Structure of the UBA Domain from Cbl-b PubMed: 18596201
Deposition date: 2007-01-24 Original release date: 2008-07-08
Authors: Zhou, Chen-Jie; Zhou, Zi-Ren; Lin, Dong-Hai; Hu, Hong-Yu
Citation: Zhou, Zi-Ren; Gao, Hong-Chang; Zhou, Chen-Jie; Chang, Yong-Gang; Hong, Jing; Song, Ai-Xin; Lin, Dong-Hai; Hu, Hong-Yu. "Differential Ubiquitin Binding of the UBA Domains from Human c-Cbl and Cbl-b: NMR Structural and Biochemical Insights" Protein Sci. 17, 1805-1814 (2008).
Assembly members:
UBA domain of Cbl-b, polymer, 46 residues, 5113.846 Da.
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):
UBA domain of Cbl-b: EAALENVDAKIAKLMGEGYA
FEEVKRALEIAQNNVEVARS
ILREFA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 113 |
| 15N chemical shifts | 42 |
| 1H chemical shifts | 258 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UBA domain of Cbl-b | 1 |
Entities:
Entity 1, UBA domain of Cbl-b 46 residues - 5113.846 Da.
| 1 | GLU | ALA | ALA | LEU | GLU | ASN | VAL | ASP | ALA | LYS | ||||
| 2 | ILE | ALA | LYS | LEU | MET | GLY | GLU | GLY | TYR | ALA | ||||
| 3 | PHE | GLU | GLU | VAL | LYS | ARG | ALA | LEU | GLU | ILE | ||||
| 4 | ALA | GLN | ASN | ASN | VAL | GLU | VAL | ALA | ARG | SER | ||||
| 5 | ILE | LEU | ARG | GLU | PHE | ALA |
Samples:
sample_1: entity, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%
sample_conditions_1: pH: 6.5; 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | 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 |
Software:
NMRDraw v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.110, Goddard - chemical shift assignment, peak picking
ARIA v2.0, Linge, O, . - data analysis, refinement, structure solution
ProcheckNMR, Laskowski and MacArthur - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAC05498 BAE36418 BAF85481 BAG52839 BAG53874 |
| EMBL | CAH18449 CAH56175 |
| GB | AAB09291 AAF13271 AAH32851 AAI50935 AAI50939 |
| REF | NP_001028410 NP_001192852 NP_598285 NP_733762 XP_001503404 |
| SP | Q13191 Q3TTA7 Q8K4S7 |
| TPG | DAA33541 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts