BMRB Entry 17945
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17945
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Title: NMR backbone assignment of a Tau protein fragment PubMed: 22072628
Deposition date: 2011-09-19 Original release date: 2011-10-28
Authors: Verdegem, Dries; Sibille, Nathalie; Wieruzeski, Jean-Michel; Lippens, Guy; Landrieu, Isabelle; Huvent, Isabelle
Citation: Sibille, Nathalie; Huvent, Isabelle; Fauquant, Caroline; Verdegem, Dries; Amniai, Laziza; Leroy, Arnaud; Wieruszeski, Jean-Michel; Lippens, Guy; Landrieu, Isabelle. "Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein." Proteins 80, 454-462 (2012).
Assembly members:
TauF4, polymer, 124 residues, 13355.4 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
Entity Sequences (FASTA):
TauF4: MHHHHHHSRSRTPSLPTPPT
REPKKVAVVRTPPKSPSSAK
SRLQTAPVPMPDLKNVKSKI
GSTENLKHQPGGGKVQIINK
KLDLSNVQSKCGSKDNIKHV
PGGGSVQIVYKPVDLSKVTS
KSGS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 214 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 99 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Polypeptide | 1 |
Entities:
Entity 1, Polypeptide 124 residues - 13355.4 Da.
The protein fragment is fused at his N-terminus to 6 Histidine residues for the purification This fragment of the neuronal Tau protein includes part of the proline rich domain [208-245] and part of the microtubule binding domain [245-324]
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | ARG | SER | ||||
| 2 | ARG | THR | PRO | SER | LEU | PRO | THR | PRO | PRO | THR | ||||
| 3 | ARG | GLU | PRO | LYS | LYS | VAL | ALA | VAL | VAL | ARG | ||||
| 4 | THR | PRO | PRO | LYS | SER | PRO | SER | SER | ALA | LYS | ||||
| 5 | SER | ARG | LEU | GLN | THR | ALA | PRO | VAL | PRO | MET | ||||
| 6 | PRO | ASP | LEU | LYS | ASN | VAL | LYS | SER | LYS | ILE | ||||
| 7 | GLY | SER | THR | GLU | ASN | LEU | LYS | HIS | GLN | PRO | ||||
| 8 | GLY | GLY | GLY | LYS | VAL | GLN | ILE | ILE | ASN | LYS | ||||
| 9 | LYS | LEU | ASP | LEU | SER | ASN | VAL | GLN | SER | LYS | ||||
| 10 | CYS | GLY | SER | LYS | ASP | ASN | ILE | LYS | HIS | VAL | ||||
| 11 | PRO | GLY | GLY | GLY | SER | VAL | GLN | ILE | VAL | TYR | ||||
| 12 | LYS | PRO | VAL | ASP | LEU | SER | LYS | VAL | THR | SER | ||||
| 13 | LYS | SER | GLY | SER |
Samples:
sample_1: TauF4, [U-95% 15N], 300-450 uM
Sample_2: TauF4, [U-95% 13C; U-95% 15N], 300-450 uM
sample_conditions_1: ionic strength: 25 mM; pH: 6.6; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | Sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | Sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | Sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | Sample_2 | isotropic | sample_conditions_1 |
| HN(CA)N | Sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - chemical shift calculation, processing
NMRPy, In house - chemical shift assignment
NMR spectrometers:
- Bruker DMX 600 MHz
Related Database Links:
| BMRB | 17920 19253 |
| EMBL | CAA32636 |
| GB | AAC04277 AAC04279 AAF97596 AAI14949 AAQ92319 |
| REF | NP_001009068 NP_001104271 NP_001116538 NP_001116539 NP_005901 |
| SP | P10636 P57786 Q5S6V2 Q5YCV9 Q5YCW0 |
| TPE | CAG26750 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts