BMRB Entry 15627
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15627
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Title: 1H, 13C and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis PubMed: 19636931
Deposition date: 2008-01-18 Original release date: 2008-04-22
Authors: Quinternet, Marc; Selme, Laure; Beaufils, Chrystel; Tsan, Pascale; Boschi-Muller, Sandrine; Averlant-Petit, Marie-Christine; Branlant, Guy; Cung, Manh-Thong
Citation: Quinternet, Marc; Selme, Laure; Beaufils, Chrystel; Tsan, Pascale; Jacob, Christophe; Boschi-Muller, Sandrine; Averlant-Petit, Marie-Christine; Branlant, Guy; Cung, Manh-Thong. "1H, 13C, and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis" Biomol. NMR Assignments 2, 85-87 (2008).
Assembly members:
nDsbD, polymer, 128 residues, Formula weight is not available
Natural source: Common Name: Micrococcus meningitidis Taxonomy ID: 487 Superkingdom: Bacteria Kingdom: not available Genus/species: Neisseria meningitidis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
nDsbD: MALDANDLLPPEKAFVPELA
VADDGVNVRFRIADGYYMYQ
AKIVGKTNPADLLGQPSFSK
GEEKEDEFFGRQTVYHHEAQ
VAFPYAKAVGEPYKLVLTYQ
GSAEAGVCYPPVDTEFDIFG
NGTYHPQT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 529 |
| 15N chemical shifts | 115 |
| 1H chemical shifts | 787 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | protein | 1 |
Entities:
Entity 1, protein 128 residues - Formula weight is not available
| 1 | MET | ALA | LEU | ASP | ALA | ASN | ASP | LEU | LEU | PRO | ||||
| 2 | PRO | GLU | LYS | ALA | PHE | VAL | PRO | GLU | LEU | ALA | ||||
| 3 | VAL | ALA | ASP | ASP | GLY | VAL | ASN | VAL | ARG | PHE | ||||
| 4 | ARG | ILE | ALA | ASP | GLY | TYR | TYR | MET | TYR | GLN | ||||
| 5 | ALA | LYS | ILE | VAL | GLY | LYS | THR | ASN | PRO | ALA | ||||
| 6 | ASP | LEU | LEU | GLY | GLN | PRO | SER | PHE | SER | LYS | ||||
| 7 | GLY | GLU | GLU | LYS | GLU | ASP | GLU | PHE | PHE | GLY | ||||
| 8 | ARG | GLN | THR | VAL | TYR | HIS | HIS | GLU | ALA | GLN | ||||
| 9 | VAL | ALA | PHE | PRO | TYR | ALA | LYS | ALA | VAL | GLY | ||||
| 10 | GLU | PRO | TYR | LYS | LEU | VAL | LEU | THR | TYR | GLN | ||||
| 11 | GLY | SER | ALA | GLU | ALA | GLY | VAL | CYS | TYR | PRO | ||||
| 12 | PRO | VAL | ASP | THR | GLU | PHE | ASP | ILE | PHE | GLY | ||||
| 13 | ASN | GLY | THR | TYR | HIS | PRO | GLN | THR |
Samples:
sample_1: nDsbD, [U-100% 13C; U-100% 15N], 0.5 mM; Potassium phosphate (KPi) 20 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 299 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
XEASY, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| EMBL | CAM08848 CAM10655 CAX49754 CBA05538 CBA06830 |
| GB | AAF41875 ABX73592 ADY95333 ADY99950 ADZ01187 |
| PIR | B81868 |
| REF | NP_274527 WP_002232751 WP_002234074 WP_002235976 WP_002238135 |
| SP | Q9JTL9 Q9JYM0 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts