BMRB Entry 17066
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PDB ID: 2l0w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17066
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Ng, Chai Ann; Hunter, Mark; Perry, Matthew; Mobli, Mehdi; Ke, Ying; Kuchel, Philip; King, Glenn; Stock, Daniela; Vandenberg, Jamie. "The N-terminal tail of hERG contains an amphipathic -helix that regulates channel deactivation." PLoS ONE 6, .-. (2011).
PubMed: 21249148
Assembly members:
Potassium_voltage-gated_channel_subfamily_H_member_2, polymer, 136 residues, 45860.719 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 Vector: PGEXT2T
Entity Sequences (FASTA):
Potassium_voltage-gated_channel_subfamily_H_member_2: SMPVRRGHVAPQNTFLDTII
RKFEGQSRKFIIANARVENC
AVIYCNDGFCELCGYSRAEV
MQRPCTCDFLHGPRTQRRAA
AQIAQALLGAEERKVEIAFY
RKDGSCFLCLVDVVPVKNED
GAVIMFILNFEVVMEK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 531 |
| 15N chemical shifts | 146 |
| 1H chemical shifts | 887 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | H_member_2 | 1 |
Entities:
Entity 1, H_member_2 136 residues - 45860.719 Da.
Residue 1 is from TEV cleavage site. This polypeptide is the N-terminal PAS domain of hERG Potassium channel.
| 1 | SER | MET | PRO | VAL | ARG | ARG | GLY | HIS | VAL | ALA | ||||
| 2 | PRO | GLN | ASN | THR | PHE | LEU | ASP | THR | ILE | ILE | ||||
| 3 | ARG | LYS | PHE | GLU | GLY | GLN | SER | ARG | LYS | PHE | ||||
| 4 | ILE | ILE | ALA | ASN | ALA | ARG | VAL | GLU | ASN | CYS | ||||
| 5 | ALA | VAL | ILE | TYR | CYS | ASN | ASP | GLY | PHE | CYS | ||||
| 6 | GLU | LEU | CYS | GLY | TYR | SER | ARG | ALA | GLU | VAL | ||||
| 7 | MET | GLN | ARG | PRO | CYS | THR | CYS | ASP | PHE | LEU | ||||
| 8 | HIS | GLY | PRO | ARG | THR | GLN | ARG | ARG | ALA | ALA | ||||
| 9 | ALA | GLN | ILE | ALA | GLN | ALA | LEU | LEU | GLY | ALA | ||||
| 10 | GLU | GLU | ARG | LYS | VAL | GLU | ILE | ALA | PHE | TYR | ||||
| 11 | ARG | LYS | ASP | GLY | SER | CYS | PHE | LEU | CYS | LEU | ||||
| 12 | VAL | ASP | VAL | VAL | PRO | VAL | LYS | ASN | GLU | ASP | ||||
| 13 | GLY | ALA | VAL | ILE | MET | PHE | ILE | LEU | ASN | PHE | ||||
| 14 | GLU | VAL | VAL | MET | GLU | LYS |
Related Database Links:
| BMRB | 16928 16946 |
| PDB | 1BYW 2L0W 2L1M 2L4R 4HP9 4HQA |
| DBJ | BAA37096 BAB19682 |
| EMBL | CAA09232 CAB09536 CAB64868 |
| GB | AAA62473 AAC53418 AAC53420 AAC53422 AAC99425 |
| REF | NP_000229 NP_001003145 NP_001092571 NP_001166444 NP_001180587 |
| SP | O08962 O35219 Q12809 Q8WNY2 Q9TSZ3 |
| TPG | DAA30311 |
| AlphaFold | O08962 O35219 Q12809 Q8WNY2 Q9TSZ3 |
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