BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 34098

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

Data sets:
Data typeCount
1H chemical shifts36

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 37 residues - 4025.676 Da.

1   LYSASNVALLYSSERLYSILEGLYSERTHR
2   GLUASNLEULYSHISGLNPROGLYGLYGLY
3   LYSVALGLNILEILEASNLYSLYSLEUASP
4   LEUSERASNVALGLNSERLYS

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:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_2isotropicsample_conditions_2
2D 1H-1H TOCSYsample_2isotropicsample_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