Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51895

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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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Name: Sequence-specific backbone assignment of the intrinsically disordered C-terminal tail of TAK1 (residues 254-344, human)
Published: 2026-01-23

Title:

Sequence-specific backbone assignment of the intrinsically disordered C-terminal tail of TAK1 (residues 254-344, human)

Deposition date:

2023-03-31

Original release date:

2026-01-23

Authors:

Machado, Luciana; Peti, Wolfgang

Citation:

Citation: Shirakawa, Karina; Parikh, Tvesha; Machado, Luciana; Poimenidou, G.; Nguyen, Hieu; Dell'Acqua, M.; Kettenbach, Arminja; Page, Rebecca; Peti, Wolfgang. "The clinical missense variant E282K in PPP3CA/calcineurin shifts substrate dephosphorylation by altering active site recruitment" Nat. Commun. ., .-. (2026).

Assembly members:

Assembly members:
entity_1, polymer, 94 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: pRP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMEGKRMSADMSEIEARIA ATTAYSKPKRGHRKTASFGN ILDVPEIVISGNGQPRRRSI QDLTVTGTEPGQVSSRSSSP SVRMITTSGPTSEK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	90
15N chemical shifts	85
1H chemical shifts	85

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TAK1	1

Entities:

Entity 1, TAK1 94 residues - Formula weight is not available

GHM are cloning artifacts

1

GLY

HIS

MET

GLU

GLY

LYS

ARG

MET

SER

ALA

2

ASP

MET

SER

GLU

ILE

GLU

ALA

ARG

ILE

ALA

3

ALA

THR

ALA

TYR

SER

LYS

PRO

LYS

ARG

4

GLY

HIS

ARG

LYS

THR

ALA

SER

PHE

GLY

ASN

5

ILE

LEU

ASP

VAL

PRO

GLU

ILE

VAL

ILE

SER

6

GLY

ASN

GLY

GLN

PRO

ARG

SER

ILE

7

GLN

ASP

LEU

THR

VAL

THR

GLY

THR

GLU

PRO

8

GLY

GLN

VAL

SER

ARG

SER

PRO

9

SER

VAL

ARG

MET

ILE

THR

SER

GLY

PRO

10

THR

SER

GLU

LYS

Samples:

sample_1: entity_1, [U-13C; U-15N], 104 uM; HEPES 20 mM; sodium chloride 50 mM; TCEP 0.5 mM; calcium chloride 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.8.2 - chemical shift assignment, peak picking

NMRPipe - processing

TOPSPIN v3.6 - processing

NMR spectrometers:

Bruker AVANCE II 500 MHz

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

BMRB Entry 51895