BMRB Entry 27012
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27012
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Citation: Smith, Roxanne; Mohanty, Biswaranjan; Williams, Martin; Scanlon, Martin; Heras, Begona. "H(N), N, C(alpha) and C(beta) assignments of the two periplasmic domains of Neisseria meningitidis DsbD" Biomol. NMR Assign. 11, 181-186 (2017).
PubMed: 28589218
Assembly members:
Oxidised_n-NmDsbD, polymer, 147 residues, Formula weight is not available
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: pMCSG7
Entity Sequences (FASTA):
Oxidised_n-NmDsbD: MHHHHHHSSGVDLGTENLYF
QSNANDLLPPEKAFVPELAV
ADDGVNVRFRIADGYYMYQA
KIVGKTDPADLLGQPSFSKG
EEKEDEFFGRQTVYHHEAQV
AFPYAKAVGEPYKLVLTYQG
CAEVGVCYPPVDTEFDISGN
GTYHPQT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 261 |
| 15N chemical shifts | 128 |
| 1H chemical shifts | 128 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | N-terminal periplasmic domain NmDsbD | 1 |
Entities:
Entity 1, N-terminal periplasmic domain NmDsbD 147 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | ||||
| 2 | VAL | ASP | LEU | GLY | THR | GLU | ASN | LEU | TYR | PHE | ||||
| 3 | GLN | SER | ASN | ALA | ASN | ASP | LEU | LEU | PRO | PRO | ||||
| 4 | GLU | LYS | ALA | PHE | VAL | PRO | GLU | LEU | ALA | VAL | ||||
| 5 | ALA | ASP | ASP | GLY | VAL | ASN | VAL | ARG | PHE | ARG | ||||
| 6 | ILE | ALA | ASP | GLY | TYR | TYR | MET | TYR | GLN | ALA | ||||
| 7 | LYS | ILE | VAL | GLY | LYS | THR | ASP | PRO | ALA | ASP | ||||
| 8 | LEU | LEU | GLY | GLN | PRO | SER | PHE | SER | LYS | GLY | ||||
| 9 | GLU | GLU | LYS | GLU | ASP | GLU | PHE | PHE | GLY | ARG | ||||
| 10 | GLN | THR | VAL | TYR | HIS | HIS | GLU | ALA | GLN | VAL | ||||
| 11 | ALA | PHE | PRO | TYR | ALA | LYS | ALA | VAL | GLY | GLU | ||||
| 12 | PRO | TYR | LYS | LEU | VAL | LEU | THR | TYR | GLN | GLY | ||||
| 13 | CYS | ALA | GLU | VAL | GLY | VAL | CYS | TYR | PRO | PRO | ||||
| 14 | VAL | ASP | THR | GLU | PHE | ASP | ILE | SER | GLY | ASN | ||||
| 15 | GLY | THR | TYR | HIS | PRO | GLN | THR |
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