BMRB Entry 34098
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34098
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Structure of Tau(254-290) bound to F-actin PubMed: 29215007
Deposition date: 2017-02-13 Original release date: 2017-12-21
Authors: Fontela, Y.; Kadavath, H.; Zweckstetter, M.
Citation: Cabrales Fontela, Y.; Kadavath, H.; Biernat, J.; Riedel, D.; Mandelkow, E.; Zweckstetter, M.. "Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau." Nat. Commun. 8, 1981-1981 (2017).
Assembly members:
entity_1, polymer, 37 residues, 4025.676 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: KNVKSKIGSTENLKHQPGGG
KVQIINKKLDLSNVQSK
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 36 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 37 residues - 4025.676 Da.
1 | LYS | ASN | VAL | LYS | SER | LYS | ILE | GLY | SER | THR | ||||
2 | GLU | ASN | LEU | LYS | HIS | GLN | PRO | GLY | GLY | GLY | ||||
3 | LYS | VAL | GLN | ILE | ILE | ASN | LYS | LYS | LEU | ASP | ||||
4 | LEU | SER | ASN | VAL | GLN | SER | LYS |
Samples:
sample_1: Tau(254-290) 800 uM; F-actin 27 uM; sodium phosphate 50 mM
sample_2: Tau(254-290) 800 uM; sodium phosphate 50 mM
sample_conditions_2: pH: 6.8; pressure: 1 atm; temperature: 278 K
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 278 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_2 |
2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_2 |
2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_2 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
SPARKY, Goddard - chemical shift assignment, peak picking
TOPSPIN, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker AvanceIII 900 MHz
- Bruker AvanceIII 800 MHz