BMRB Entry 26309
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26309
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Title: Backbone 1H, 15N, and 13C resonance assignments of the Phafin2 PH domain
Deposition date: 2021-08-03 Original release date: 2022-05-12
Authors: Ellena, Jeffrey; Tang, Tuo-Xian; Shanaiah, Narasimhamurthy; Capelluto, Daniel
Citation: Ellena, Jeffrey; Tang, Tuo-Xian; Shanaiah, Narasimhamurthy; Capelluto, Daniel. "Backbone 1 H, 15 N, and 13 C resonance assignments of the Phafin2 pleckstrin homology domain" Biomol. NMR Assign. 16, 27-30 (2022).
Assembly members:
Human Phafin2 pleckstrin homology domain, polymer, 140 residues, Formula weight is not available
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 Vector: pGEX6P1
Entity Sequences (FASTA):
Human Phafin2 pleckstrin homology domain: GPLGSMVDRLANSEANTRRI
SIVENCFGAAGQPLTIPGRV
LIGEGVLTKLCRKKPKARQF
FLFNDILVYGNIVIQKKKYN
KQHIIPLENVTIDSIKDEGD
LRNGWLIKTPTKSFAVYAAT
ATEKSEWMNHINKCVTDLLS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 407 |
15N chemical shifts | 132 |
1H chemical shifts | 132 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Phafin2 PH domain | 1 |
Entities:
Entity 1, Phafin2 PH domain 140 residues - Formula weight is not available
The first five residues of the sequence (GPLGS) are non-native amino acids that remained from HRV-3C protease cleavage of the GST tag. The remaining sequence belongs to the Phafin2 PH domain (residues 1-135).
1 | GLY | PRO | LEU | GLY | SER | MET | VAL | ASP | ARG | LEU | |
2 | ALA | ASN | SER | GLU | ALA | ASN | THR | ARG | ARG | ILE | |
3 | SER | ILE | VAL | GLU | ASN | CYS | PHE | GLY | ALA | ALA | |
4 | GLY | GLN | PRO | LEU | THR | ILE | PRO | GLY | ARG | VAL | |
5 | LEU | ILE | GLY | GLU | GLY | VAL | LEU | THR | LYS | LEU | |
6 | CYS | ARG | LYS | LYS | PRO | LYS | ALA | ARG | GLN | PHE | |
7 | PHE | LEU | PHE | ASN | ASP | ILE | LEU | VAL | TYR | GLY | |
8 | ASN | ILE | VAL | ILE | GLN | LYS | LYS | LYS | TYR | ASN | |
9 | LYS | GLN | HIS | ILE | ILE | PRO | LEU | GLU | ASN | VAL | |
10 | THR | ILE | ASP | SER | ILE | LYS | ASP | GLU | GLY | ASP | |
11 | LEU | ARG | ASN | GLY | TRP | LEU | ILE | LYS | THR | PRO | |
12 | THR | LYS | SER | PHE | ALA | VAL | TYR | ALA | ALA | THR | |
13 | ALA | THR | GLU | LYS | SER | GLU | TRP | MET | ASN | HIS | |
14 | ILE | ASN | LYS | CYS | VAL | THR | ASP | LEU | LEU | SER |
Samples:
sample_1: Human Phafin2 pleckstrin homology domain, [U-100% 13C; U-100% 15N], 300 uM; d4-citrate, [U-98% 2H], 5 mM; NaCl 100 mM; DTT, [U-2H], 5 mM; sodium acetate, [U-2H], 5 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D NHSQC | 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 HNCACO | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.2.7 - collection
NMRPipe v10.9_rev2021.005.11.52 - data visualization, processing
SMILE v10.9_rev2021.005.11.52 - reconstruction of non-uniformly sampled data
NMRFAM-SPARKY vBuild_01-26-2021 - visualization and analysis of data
NMRbox v7/1/21 - provided all software used and server for software execution
NMR spectrometers:
- Bruker AVANCE III 800 MHz MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts