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 25475

Title: Structure of Tau(267-312) bound to Microtubules   PubMed: 26094605

Authors: Kadavath, Harindranath; Jaremko, Mariusz; Jaremko, Lukasz; Zweckstetter, Markus

Citation: Kadavath, Harindranath; Jaremko, Mariusz; Jaremko, Lukasz; Biernat, Jacek; Mandelkow, Eckhard; Zweckstetter, Markus. "Folding of the Tau Protein on Microtubules"  Angew. Chem. Int. Ed. Engl. 54, 10347-10351 (2015).

Assembly members:
entity, polymer, 46 residues, 4892.728 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: KHQPGGGKVQIINKKLDLSN VQSKCGSKDNIKHVPGGGSV QIVYKP

Data sets:
Data typeCount
1H chemical shifts43

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 46 residues - 4892.728 Da.

1   LYSHISGLNPROGLYGLYGLYLYSVALGLN
2   ILEILEASNLYSLYSLEUASPLEUSERASN
3   VALGLNSERLYSCYSGLYSERLYSASPASN
4   ILELYSHISVALPROGLYGLYGLYSERVAL
5   GLNILEVALTYRLYSPRO

Samples:

sample_1: sodium phosphate 50 mM; entity 1 mM; H2O 90%; D2O 10%

sample_2: sodium phosphate 50 mM; entity 1 mM; microtubules 50 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 6.8; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH v2.33, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution

SPARKY, Goddard - data analysis, peak picking

TOPSPIN v3.0, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz

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