BMRB Entry 19670
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19670
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Title: Solution structure of lysine-free (K0) ubiquitin PubMed: 24591328
Deposition date: 2013-12-09 Original release date: 2014-03-31
Authors: Huang, Tao; Li, Jess; Byrd, Andrew
Citation: Huang, Tao; Li, Jess; Byrd, R. Andrew. "Solution structure of lysine-free (K0) ubiquitin." Protein Sci. 23, 662-667 (2014).
Assembly members:
entity, polymer, 76 residues, 8773.008 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):
entity: MQIFVRTLTGRTITLEVEPS
DTIENVRARIQDREGIPPDQ
QRLIFAGRQLEDGRTLSDYN
IQRESTLHLVLRLRGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 219 |
| 15N chemical shifts | 70 |
| 1H chemical shifts | 258 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | lysine-free (K0) ubiquitin | 1 |
Entities:
Entity 1, lysine-free (K0) ubiquitin 76 residues - 8773.008 Da.
| 1 | MET | GLN | ILE | PHE | VAL | ARG | THR | LEU | THR | GLY | ||||
| 2 | ARG | THR | ILE | THR | LEU | GLU | VAL | GLU | PRO | SER | ||||
| 3 | ASP | THR | ILE | GLU | ASN | VAL | ARG | ALA | ARG | ILE | ||||
| 4 | GLN | ASP | ARG | GLU | GLY | ILE | PRO | PRO | ASP | GLN | ||||
| 5 | GLN | ARG | LEU | ILE | PHE | ALA | GLY | ARG | GLN | LEU | ||||
| 6 | GLU | ASP | GLY | ARG | THR | LEU | SER | ASP | TYR | ASN | ||||
| 7 | ILE | GLN | ARG | GLU | SER | THR | LEU | HIS | LEU | VAL | ||||
| 8 | LEU | ARG | LEU | ARG | GLY | GLY |
Samples:
sample_1: K-free ubiquitin, [U-13C; U-15N], 0.5 mM; TRIS 50 mM; D2O, [U-100% 2H], 5%; H2O 95%
sample_conditions_1: ionic strength: 0.01 M; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 HBHA(CO)NH | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
CS-Rosetta, Shen, Vernon, Baker and Bax - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts