BMRB Entry 18669
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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/BMR18669
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Title: Solution structure of the Get5 ubiquitin-like domain PubMed: 23142665
Deposition date: 2012-08-19 Original release date: 2012-11-20
Authors: Chartron, Justin; VanderVelde, David; Clemons, William
Citation: Chartron, Justin; VanderVelde, David; Clemons, William. "Structures of the Sgt2/SGTA dimerization domain with the Get5/UBL4A UBL domain reveal an interaction that forms a conserved dynamic interface." Cell Rep. 2, 1620-1632 (2012).
Assembly members:
Get5, polymer, 87 residues, 9999.781 Da.
Natural source: Common Name: Baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Get5: MVHLTLKKIQAPKFSIEHDF
SPSDTILQIKQHLISEEKAS
HISEIKLLLKGKVLHDNLFL
SDLKVTPANSTITVMIKPNL
EHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 270 |
15N chemical shifts | 78 |
1H chemical shifts | 550 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Get5 | 1 |
Entities:
Entity 1, Get5 87 residues - 9999.781 Da.
1 | MET | VAL | HIS | LEU | THR | LEU | LYS | LYS | ILE | GLN | ||||
2 | ALA | PRO | LYS | PHE | SER | ILE | GLU | HIS | ASP | PHE | ||||
3 | SER | PRO | SER | ASP | THR | ILE | LEU | GLN | ILE | LYS | ||||
4 | GLN | HIS | LEU | ILE | SER | GLU | GLU | LYS | ALA | SER | ||||
5 | HIS | ILE | SER | GLU | ILE | LYS | LEU | LEU | LEU | LYS | ||||
6 | GLY | LYS | VAL | LEU | HIS | ASP | ASN | LEU | PHE | LEU | ||||
7 | SER | ASP | LEU | LYS | VAL | THR | PRO | ALA | ASN | SER | ||||
8 | THR | ILE | THR | VAL | MET | ILE | LYS | PRO | ASN | LEU | ||||
9 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Get5, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 6.1; pressure: 1 atm; temperature: 297.5 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N 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 (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
Analysis, CCPN - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS+, Cornilescu, Delaglio and Bax - data analysis
ARIA v2.3, Linge, O, . - refinement, structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
BMRB | 18342 18671 |
PDB | |
DBJ | GAA26218 |
EMBL | CAA88151 CAA99130 CAY86179 |
GB | AHY77206 AJP41438 AJT70857 AJT71348 AJT71834 |
REF | NP_014530 |
SP | Q12285 |
TPG | DAA10672 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts