BMRB Entry 34099

Name: Structure of Tau(292-319) bound to F-actin
Published: 2017-12-21

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PDB ID: 5n5b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34099
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Structure of Tau(292-319) bound to F-actin

Deposition date:

2017-02-13

Original release date:

2017-12-21

Authors:

Fontela, Y.; Kadavath, H.; Zweckstetter, M.

Citation:

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).
PubMed: 29215007

Assembly members:

Assembly members:
entity_1, polymer, 28 residues, 2928.364 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSKDNIKHVPGGGSVQIVYK PVDLSKVT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	32

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 28 residues - 2928.364 Da.

1

GLY

SER

LYS

ASP

ASN

ILE

LYS

HIS

VAL

PRO

2

GLY

SER

VAL

GLN

ILE

VAL

TYR

LYS

3

PRO

VAL

ASP

LEU

SER

LYS

VAL

THR

Samples:

sample_1: Tau(292-319) 800 uM; F-actin 27 uM; sodium phosphate 50 mM

sample_2: sodium phosphate 50 mM; Tau(254-290) 800 uM

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