BMRB Entry 51716
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51716
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Title: Partial Backbone Assignment of The Q163C/Q309C Mutant of aMI-domain in the Co2+-Bound Form PubMed: 36696377
Deposition date: 2022-11-30 Original release date: 2023-04-04
Authors: Nguyen, Hoa; Wang, Xu
Citation: Nguyen, Hoa; Jing, Tianwei; Wang, Xu. "The Q163C/Q309C mutant of alphaMI-domain is an active variant suitable for NMR characterization" PLoS One 18, e0280778-e0280778 (2023).
Assembly members:
entity_1, polymer, 194 residues, Formula weight is not available
entity_GLU, non-polymer, 147.129 Da.
entity_CO, non-polymer, 58.933 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: pET-15b
Entity Sequences (FASTA):
entity_1: EDSDIAFLIDGSGSIIPHDF
RRMKEFVSTVMECLKKSKTL
FSLMQYSEEFRIHFTFKEFQ
NNPNPRSLVKPITQLLGRTH
TATGIRKVVRELFNITNGAR
KNAFKILVVITDGEKFGDPL
GYEDVIPEADREGVIRYVIG
VGDAFRSEKSRQELNTIASK
PPRDHVFQVNNFEALKTICN
QLREKIFAIEGTQT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 72 |
| 15N chemical shifts | 38 |
| 1H chemical shifts | 38 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Q163C | 1 |
| 2 | Glu | 2 |
| 3 | Co | 3 |
Entities:
Entity 1, Q163C 194 residues - Formula weight is not available
Contains the mutations Q163C and Q309C to create the disulfide bond needed to
| 1 | GLU | ASP | SER | ASP | ILE | ALA | PHE | LEU | ILE | ASP | ||||
| 2 | GLY | SER | GLY | SER | ILE | ILE | PRO | HIS | ASP | PHE | ||||
| 3 | ARG | ARG | MET | LYS | GLU | PHE | VAL | SER | THR | VAL | ||||
| 4 | MET | GLU | CYS | LEU | LYS | LYS | SER | LYS | THR | LEU | ||||
| 5 | PHE | SER | LEU | MET | GLN | TYR | SER | GLU | GLU | PHE | ||||
| 6 | ARG | ILE | HIS | PHE | THR | PHE | LYS | GLU | PHE | GLN | ||||
| 7 | ASN | ASN | PRO | ASN | PRO | ARG | SER | LEU | VAL | LYS | ||||
| 8 | PRO | ILE | THR | GLN | LEU | LEU | GLY | ARG | THR | HIS | ||||
| 9 | THR | ALA | THR | GLY | ILE | ARG | LYS | VAL | VAL | ARG | ||||
| 10 | GLU | LEU | PHE | ASN | ILE | THR | ASN | GLY | ALA | ARG | ||||
| 11 | LYS | ASN | ALA | PHE | LYS | ILE | LEU | VAL | VAL | ILE | ||||
| 12 | THR | ASP | GLY | GLU | LYS | PHE | GLY | ASP | PRO | LEU | ||||
| 13 | GLY | TYR | GLU | ASP | VAL | ILE | PRO | GLU | ALA | ASP | ||||
| 14 | ARG | GLU | GLY | VAL | ILE | ARG | TYR | VAL | ILE | GLY | ||||
| 15 | VAL | GLY | ASP | ALA | PHE | ARG | SER | GLU | LYS | SER | ||||
| 16 | ARG | GLN | GLU | LEU | ASN | THR | ILE | ALA | SER | LYS | ||||
| 17 | PRO | PRO | ARG | ASP | HIS | VAL | PHE | GLN | VAL | ASN | ||||
| 18 | ASN | PHE | GLU | ALA | LEU | LYS | THR | ILE | CYS | ASN | ||||
| 19 | GLN | LEU | ARG | GLU | LYS | ILE | PHE | ALA | ILE | GLU | ||||
| 20 | GLY | THR | GLN | THR |
Entity 2, Glu - C5 H9 N O4 - 147.129 Da.
| 1 | GLU |
Entity 3, Co - Co - 58.933 Da.
| 1 | CO |
Samples:
sample_1: alphaM-I-domain, [U-100% 13C; U-100% 15N; U-80% 2H], 0.25 mM; sodium glutamate 10 mM; Cobalt Chloride 1 mM; HEPES 20 mM; sodium chloride 0.1 M
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
NMRViewJ - data analysis
I-PINE - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 850 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts