BMRB Entry 18342
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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/BMR18342
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Title: Backbone and sidechain assignments for Get5_UBL domain PubMed: 23001946
Deposition date: 2012-03-21 Original release date: 2012-11-15
Authors: Simon, Aline; Simpson, Peter; Isaacson, Rivka
Citation: Simon, Aline; Simpson, Peter; Hawthorne, William; Hale, Lisa; Goldstone, Rachael; Isaacson, Rivka. "1H, 13C and 15N assignments of Sgt2N-terminal dimerisation domain and its binding partner, Get5 Ubiquitin-like domain." Biomol. NMR Assignments 7, 271-274 (2013).
Assembly members:
Get5_ubl, polymer, 97 residues, 10963.5 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_ubl: AHHHHHHVDDDDKMDNAAVH
LTLKKIQAPKFSIEHDFSPS
DTILQIKQHLISEEKASHIS
EIKLLLKGKVLHDNLFLSDL
KVTPANSTITVMIKPNP
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 383 |
15N chemical shifts | 82 |
1H chemical shifts | 601 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Get5_ubl | 1 |
Entities:
Entity 1, Get5_ubl 97 residues - 10963.5 Da.
1 | ALA | HIS | HIS | HIS | HIS | HIS | HIS | VAL | ASP | ASP | ||||
2 | ASP | ASP | LYS | MET | ASP | ASN | ALA | ALA | VAL | HIS | ||||
3 | LEU | THR | LEU | LYS | LYS | ILE | GLN | ALA | PRO | LYS | ||||
4 | PHE | SER | ILE | GLU | HIS | ASP | PHE | SER | PRO | SER | ||||
5 | ASP | THR | ILE | LEU | GLN | ILE | LYS | GLN | HIS | LEU | ||||
6 | ILE | SER | GLU | GLU | LYS | ALA | SER | HIS | ILE | SER | ||||
7 | GLU | ILE | LYS | LEU | LEU | LEU | LYS | GLY | LYS | VAL | ||||
8 | LEU | HIS | ASP | ASN | LEU | PHE | LEU | SER | ASP | LEU | ||||
9 | LYS | VAL | THR | PRO | ALA | ASN | SER | THR | ILE | THR | ||||
10 | VAL | MET | ILE | LYS | PRO | ASN | PRO |
Samples:
sample_1: Get5_ubl, [U-98% 13C; U-98% 15N], 700 uM; MES 100 mM; potassium chloride 150 mM; TCEP 0.5 mM; H2O 90%; D2O 10%
sample_2: Get5_ubl, [U-98% 13C; U-98% 15N], 700 uM; MES 100 mM; potassium chloride 150 mM; TCEP 0.5 mM; D2O 100%
sample_conditions_1: ionic strength: 0.25 M; pH: 6; pressure: 1 atm; temperature: 308 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 HBHA(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 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D (H)CCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
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