BMRB Entry 18419
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18419
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Citation: Berry, Jamie-Lee; Phelan, Marie; Collins, Richard; Adomavicius, Tomas; Tnjum, Tone; Frye, Stefan; Bird, Louise; Owens, Ray; Ford, Robert; Lian, Lu-Yun; Derrick, Jeremy. "Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis." PLoS Pathog. 8, .-. (2012).
PubMed: 23028322
Assembly members:
NmPilQ_B2, polymer, 138 residues, 15181.3338 Da.
Natural source: Common Name: Neisseria meningitidis Taxonomy ID: 487 Superkingdom: Bacteria Kingdom: not available Genus/species: Neisseria meningitidis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
NmPilQ_B2: MGSSHHHHHHGLVPRGSHMA
SMTGGQQMGRGSKQTNIDFR
KDGKNAGIIELAALGFAGQP
DISQQHDHIIVTLKNHTLPT
TLQRSLDVADFKTPVQKVTL
KRLNNDTQLIITTAGNWELV
NKSAAPGYFTFQVLPKKQ
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 831 |
| 13C chemical shifts | 529 |
| 15N chemical shifts | 124 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NmPilQ_B2 | 1 |
Entities:
Entity 1, NmPilQ_B2 138 residues - 15181.3338 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | MET | ALA | ||||
| 3 | SER | MET | THR | GLY | GLY | GLN | GLN | MET | GLY | ARG | ||||
| 4 | GLY | SER | LYS | GLN | THR | ASN | ILE | ASP | PHE | ARG | ||||
| 5 | LYS | ASP | GLY | LYS | ASN | ALA | GLY | ILE | ILE | GLU | ||||
| 6 | LEU | ALA | ALA | LEU | GLY | PHE | ALA | GLY | GLN | PRO | ||||
| 7 | ASP | ILE | SER | GLN | GLN | HIS | ASP | HIS | ILE | ILE | ||||
| 8 | VAL | THR | LEU | LYS | ASN | HIS | THR | LEU | PRO | THR | ||||
| 9 | THR | LEU | GLN | ARG | SER | LEU | ASP | VAL | ALA | ASP | ||||
| 10 | PHE | LYS | THR | PRO | VAL | GLN | LYS | VAL | THR | LEU | ||||
| 11 | LYS | ARG | LEU | ASN | ASN | ASP | THR | GLN | LEU | ILE | ||||
| 12 | ILE | THR | THR | ALA | GLY | ASN | TRP | GLU | LEU | VAL | ||||
| 13 | ASN | LYS | SER | ALA | ALA | PRO | GLY | TYR | PHE | THR | ||||
| 14 | PHE | GLN | VAL | LEU | PRO | LYS | LYS | GLN |
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