BMRB Entry 25475

Name: Structure of Tau(267-312) bound to Microtubules
Published: 2015-07-13

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PDB ID: 2mz7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25475
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Structure of Tau(267-312) bound to Microtubules

Deposition date:

2015-02-06

Original release date:

2015-07-13

Authors:

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

Citation:

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).
PubMed: 26094605

Assembly members:

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	43

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 46 residues - 4892.728 Da.

1

LYS

HIS

GLN

PRO

GLY

LYS

VAL

GLN

2

ILE

ASN

LYS

LEU

ASP

LEU

SER

ASN

3

VAL

GLN

SER

LYS

CYS

GLY

SER

LYS

ASP

ASN

4

ILE

LYS

HIS

VAL

PRO

GLY

SER

VAL

5

GLN

ILE

VAL

TYR

LYS

PRO

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:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_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