BMRB Entry 27533
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27533
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Title: NBPF-15 HLS2-domain PubMed: 31264103
Deposition date: 2018-07-05 Original release date: 2019-07-02
Authors: Issaian, Aaron; Hansen, Kirk; Sikela, James; Vogeli, Beat; Henen, Morkos
Citation: Issaian, Aaron; Schmitt, Lauren; Born, Alexandra; Nichols, Parker; Sikela, James; Hansen, Kirk; Vogeli, Beat; Henen, Morkos. "Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains" Biomol. NMR Assign. 13, 339-343 (2019).
Assembly members:
HLS-2, polymer, 106 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: pET-21
Entity Sequences (FASTA):
HLS-2: SAAAASSASLEIDMDEIEKY
QEVEEDQDPSCPRLSRELLD
EKEPEVLQDSLDRCYSTPSD
YLELPDLGQPYSSAVYSLEE
QYLGLALDVDRIKKDQEELE
HHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 229 |
15N chemical shifts | 77 |
1H chemical shifts | 77 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HLS2 | 1 |
Entities:
Entity 1, HLS2 106 residues - Formula weight is not available
The numbering goes from 1-106 where 1-11 and 100-106 are cloning artifact and tags while actual protein is 12-99.
1 | SER | ALA | ALA | ALA | ALA | SER | SER | ALA | SER | LEU | ||||
2 | GLU | ILE | ASP | MET | ASP | GLU | ILE | GLU | LYS | TYR | ||||
3 | GLN | GLU | VAL | GLU | GLU | ASP | GLN | ASP | PRO | SER | ||||
4 | CYS | PRO | ARG | LEU | SER | ARG | GLU | LEU | LEU | ASP | ||||
5 | GLU | LYS | GLU | PRO | GLU | VAL | LEU | GLN | ASP | SER | ||||
6 | LEU | ASP | ARG | CYS | TYR | SER | THR | PRO | SER | ASP | ||||
7 | TYR | LEU | GLU | LEU | PRO | ASP | LEU | GLY | GLN | PRO | ||||
8 | TYR | SER | SER | ALA | VAL | TYR | SER | LEU | GLU | GLU | ||||
9 | GLN | TYR | LEU | GLY | LEU | ALA | LEU | ASP | VAL | ASP | ||||
10 | ARG | ILE | LYS | LYS | ASP | GLN | GLU | GLU | LEU | GLU | ||||
11 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: HLS-2, [U-99% 13C; U-99% 15N], 320 uM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 5 mM
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 273 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HCACO | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - peak picking, processing
SPARKY, Goddard - chemical shift assignment, data analysis
NMR spectrometers:
- Varian INOVA 900 MHz
- Varian INOVA 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts