Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17831
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Mavridou, Despoina; Saridakis, Emmanuel; Kritsiligkou, Paraskevi; Goddard, Alan; Stevens, Julie; Ferguson, Stuart; Redfield, Christina. "Oxidation state-dependent protein-protein interactions in disulfide cascades." J. Biol. Chem. 286, 24943-24956 (2011).
PubMed: 21543317
Assembly members:
nDsbD-ox, polymer, 139 residues, 15604.5 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b(+)
Data type | Count |
13C chemical shifts | 475 |
15N chemical shifts | 119 |
1H chemical shifts | 746 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | nDsbD-ox | 1 |
Entity 1, nDsbD-ox 139 residues - 15604.5 Da.
Residues L2-V132 of the native sequence have been deposited. This is the N-terminal periplasmic domain of a membrane protein. The N-terminal residues MDT are a result of the cloning process. Residues G133-R137 remain after thrombin cleavage of the affinity tag.
1 | MET | ASP | THR | LEU | PHE | ASP | ALA | PRO | GLY | ARG | ||||
2 | SER | GLN | PHE | VAL | PRO | ALA | ASP | GLN | ALA | PHE | ||||
3 | ALA | PHE | ASP | PHE | GLN | GLN | ASN | GLN | HIS | ASP | ||||
4 | LEU | ASN | LEU | THR | TRP | GLN | ILE | LYS | ASP | GLY | ||||
5 | TYR | TYR | LEU | TYR | ARG | LYS | GLN | ILE | ARG | ILE | ||||
6 | THR | PRO | GLU | HIS | ALA | LYS | ILE | ALA | ASP | VAL | ||||
7 | GLN | LEU | PRO | GLN | GLY | VAL | TRP | HIS | GLU | ASP | ||||
8 | GLU | PHE | TYR | GLY | LYS | SER | GLU | ILE | TYR | ARG | ||||
9 | ASP | ARG | LEU | THR | LEU | PRO | VAL | THR | ILE | ASN | ||||
10 | GLN | ALA | SER | ALA | GLY | ALA | THR | LEU | THR | VAL | ||||
11 | THR | TYR | GLN | GLY | CYS | ALA | ASP | ALA | GLY | PHE | ||||
12 | CYS | TYR | PRO | PRO | GLU | THR | LYS | THR | VAL | PRO | ||||
13 | LEU | SER | GLU | VAL | VAL | ALA | ASN | ASN | ALA | ALA | ||||
14 | PRO | GLN | PRO | VAL | GLY | LEU | VAL | PRO | ARG |
sample_1: nDsbD-ox, [U-98% 15N], 0.5 1.0 mM; H2O 95%; D2O 5%
sample_2: nDsbD-ox, [U-98% 13C; U-98% 15N], 0.5 1.0 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC NH2 only | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N HSQC-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CcpNMR, CCPN - chemical shift assignment
BMRB | 17830 |
PDB | |
DBJ | BAB38540 BAE78138 BAG66862 BAG79959 BAI28440 |
EMBL | CAA54781 CAA85375 CAQ34485 CAR01112 CAR05872 |
GB | AAA97035 AAC77096 AAG59335 AAN45708 AAN83640 |
REF | NP_313144 NP_418559 NP_710001 WP_000068901 WP_000068902 |
SP | P36655 P58162 Q0SXE3 Q0T9Q5 Q1R3C4 |
AlphaFold | Q0T9Q5 Q0SXE3 Q1R3C4 P58162 P36655 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks