BMRB Entry 50130

Name: Backbone assignments of Tau fragment (225-324) with P301L mutation
Published: 2020-08-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50130

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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:

Backbone assignments of Tau fragment (225-324) with P301L mutation

Deposition date:

2019-12-15

Original release date:

2020-08-03

Authors:

Kawasaki, Ryosuke

Citation:

Citation: Kawasaki, Ryosuke; Tate, Shin-Ichi. "Impact of the Hereditary P301L Mutation on the Correlated Conformational Dynamics of Human Tau Protein Revealed by the Paramagnetic Relaxation Enhancement NMR Experiments" Int. J. Mol. Sci. 21, .-. (2020).
PubMed: 32486218

Assembly members:

Assembly members:
entity_1, polymer, 104 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMKVAVVRTPPKSPSSAK SRLQTAPVPMPDLKNVKSKI GSTENLKHQPGGGKVQIINK KLDLSNVQSKCGSKDNIKHV LGGGSVQIVYKPVDLSKVTS KCGS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	424
15N chemical shifts	101
1H chemical shifts	93

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	P301L TauF4d fragment	1

Entities:

Entity 1, P301L TauF4d fragment 104 residues - Formula weight is not available

1

GLY

SER

HIS

MET

LYS

VAL

ALA

VAL

ARG

2

THR

PRO

LYS

SER

PRO

SER

ALA

LYS

3

SER

ARG

LEU

GLN

THR

ALA

PRO

VAL

PRO

MET

4

PRO

ASP

LEU

LYS

ASN

VAL

LYS

SER

LYS

ILE

5

GLY

SER

THR

GLU

ASN

LEU

LYS

HIS

GLN

PRO

6

GLY

LYS

VAL

GLN

ILE

ASN

LYS

7

LYS

LEU

ASP

LEU

SER

ASN

VAL

GLN

SER

LYS

8

CYS

GLY

SER

LYS

ASP

ASN

ILE

LYS

HIS

VAL

9

LEU

GLY

SER

VAL

GLN

ILE

VAL

TYR

10

LYS

PRO

VAL

ASP

LEU

SER

LYS

VAL

THR

SER

11

LYS

CYS

GLY

SER

Samples:

sample_1: P301L TauF4d fragment, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS 50 mM; DTT 1 mM; sodium azide 0.03%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 285 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D (H)CC(CO)NNH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks