BMRB Entry 53400

Name: tau321-391 chemical shifts
Published: 2025-11-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53400

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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:

tau321-391 chemical shifts

Deposition date:

2025-10-22

Original release date:

2025-11-25

Authors:

Cehlar, Ondrej; Njemoga, Stefana; Kaderavek, Pavel; Volko, Viliam

Citation:

Citation: Cehlar, Ondrej. "Pre-aggeregation conformation of disorderd protein tau recognized by the Alzheimer's disease specific antibody DC11" Protein Sci. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 71 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-17b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KCGSLGNIHHKPGGGQVEVK SEKLDFKDRVQSKIGSLDNI THVPGGGNKKIETHKLTFRE NAKAKTDHGAE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	121
15N chemical shifts	61
1H chemical shifts	61

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	tau321-391	1

Entities:

Entity 1, tau321-391 71 residues - Formula weight is not available

1

LYS

CYS

GLY

SER

LEU

GLY

ASN

ILE

HIS

2

LYS

PRO

GLY

GLN

VAL

GLU

VAL

LYS

3

SER

GLU

LYS

LEU

ASP

PHE

LYS

ASP

ARG

VAL

4

GLN

SER

LYS

ILE

GLY

SER

LEU

ASP

ASN

ILE

5

THR

HIS

VAL

PRO

GLY

ASN

LYS

6

ILE

GLU

THR

HIS

LYS

LEU

THR

PHE

ARG

GLU

7

ASN

ALA

LYS

ALA

LYS

THR

ASP

HIS

GLY

ALA

8

GLU

Samples:

sample_1: tau321-391, [U-100% 13C; U-100% 15N], 0.5 mM; phospahte buffer saline (PBS) mM; DTT 5 mM

sample_conditions_1: ionic strength: 161.7 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 950 MHz

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