BMRB Entry 50549
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50549
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Ayyappan, Shine; Dharan, Pooja; Krishnan, Arya; Marira, Renjith; Lambert, Mahil; Manna, Tapas; Vijayan, Vinesh. "SxIP binding disrupts the constitutive homodimer interface of EB1 and stabilizes EB1 monomer" Biophys. J. 120, 2019-2029 (2021).
PubMed: 33737159
Assembly members:
entity_1, polymer, 268 residues, Formula weight is not available
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: pET28a
Entity Sequences (FASTA):
entity_1: MAVNVYSTSVTSDNLSRHDM
LAWINESLQLNLTKIEQLCS
GAAYCQFMDMLFPGSIALKK
VKFQAKLEHEYIQNFKILQA
GFKRMGVDKIIPVDKLVKGK
FQDNFEFVQWFKKFFDANYD
GKDYDPVAARQGQETAVAPS
LVAPALNKPKKPLTSSSAAP
QRPISTQRTAAAPKAGPGVV
RKNPGVGNGDDEAAELMQQV
NVLKLTVEDLEKERDFYFGK
LRNIELICQENEGENDPVLQ
RIVDILYATDEGFVIPDEGG
PQEEQEEY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 237 |
| 15N chemical shifts | 124 |
| 1H chemical shifts | 124 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EB1 | 1 |
Entities:
Entity 1, EB1 268 residues - Formula weight is not available
| 1 | MET | ALA | VAL | ASN | VAL | TYR | SER | THR | SER | VAL | ||||
| 2 | THR | SER | ASP | ASN | LEU | SER | ARG | HIS | ASP | MET | ||||
| 3 | LEU | ALA | TRP | ILE | ASN | GLU | SER | LEU | GLN | LEU | ||||
| 4 | ASN | LEU | THR | LYS | ILE | GLU | GLN | LEU | CYS | SER | ||||
| 5 | GLY | ALA | ALA | TYR | CYS | GLN | PHE | MET | ASP | MET | ||||
| 6 | LEU | PHE | PRO | GLY | SER | ILE | ALA | LEU | LYS | LYS | ||||
| 7 | VAL | LYS | PHE | GLN | ALA | LYS | LEU | GLU | HIS | GLU | ||||
| 8 | TYR | ILE | GLN | ASN | PHE | LYS | ILE | LEU | GLN | ALA | ||||
| 9 | GLY | PHE | LYS | ARG | MET | GLY | VAL | ASP | LYS | ILE | ||||
| 10 | ILE | PRO | VAL | ASP | LYS | LEU | VAL | LYS | GLY | LYS | ||||
| 11 | PHE | GLN | ASP | ASN | PHE | GLU | PHE | VAL | GLN | TRP | ||||
| 12 | PHE | LYS | LYS | PHE | PHE | ASP | ALA | ASN | TYR | ASP | ||||
| 13 | GLY | LYS | ASP | TYR | ASP | PRO | VAL | ALA | ALA | ARG | ||||
| 14 | GLN | GLY | GLN | GLU | THR | ALA | VAL | ALA | PRO | SER | ||||
| 15 | LEU | VAL | ALA | PRO | ALA | LEU | ASN | LYS | PRO | LYS | ||||
| 16 | LYS | PRO | LEU | THR | SER | SER | SER | ALA | ALA | PRO | ||||
| 17 | GLN | ARG | PRO | ILE | SER | THR | GLN | ARG | THR | ALA | ||||
| 18 | ALA | ALA | PRO | LYS | ALA | GLY | PRO | GLY | VAL | VAL | ||||
| 19 | ARG | LYS | ASN | PRO | GLY | VAL | GLY | ASN | GLY | ASP | ||||
| 20 | ASP | GLU | ALA | ALA | GLU | LEU | MET | GLN | GLN | VAL | ||||
| 21 | ASN | VAL | LEU | LYS | LEU | THR | VAL | GLU | ASP | LEU | ||||
| 22 | GLU | LYS | GLU | ARG | ASP | PHE | TYR | PHE | GLY | LYS | ||||
| 23 | LEU | ARG | ASN | ILE | GLU | LEU | ILE | CYS | GLN | GLU | ||||
| 24 | ASN | GLU | GLY | GLU | ASN | ASP | PRO | VAL | LEU | GLN | ||||
| 25 | ARG | ILE | VAL | ASP | ILE | LEU | TYR | ALA | THR | ASP | ||||
| 26 | GLU | GLY | PHE | VAL | ILE | PRO | ASP | GLU | GLY | GLY | ||||
| 27 | PRO | GLN | GLU | GLU | GLN | GLU | GLU | TYR |
Samples:
sample_1: EB1, [U-13C; U-15N; U-2H], 1 mM; PBS 50 mM; KCl 300 mM; DTT 1 mM
sample_conditions_1: ionic strength: 0.3 M; pH: 6.9; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks