BMRB Entry 28065

Name: Backbone N, HN, CO and CA Chemical Shift Assignments for Tau (1-239)
Published: 2020-10-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28065

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Backbone N, HN, CO and CA Chemical Shift Assignments for Tau (1-239) PubMed: 32832664

Deposition date: 2020-01-27 Original release date: 2020-10-14

Authors: Ibanez de Opakua, Alain; Zweckstetter, Markus; Cima-Omori, Maria Sol

Citation: Ukmar-Godec, Tina; Fang, Pan; Ibanez de Opakua, Alain; Henneberg, Fabian; Godec, Aljaz; Pan, Kuan-Ting; Cima-Omori, Maria Sol; Chari, Ashwin; Mandelkow, Eckhard; Urlaub, Henning; Zweckstetter, Markus. "PProteasomal degradation of the intrinsically disordered protein tau at single-residue resolution" Sci. Adv. 6, eaba3916-eaba3916 (2020).

Assembly members:
Tau_(1-239), polymer, 239 residues, Formula weight is not available

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pNG2

Entity Sequences (FASTA):
Tau_(1-239): MAEPRQEFEVMEDHAGTYGL GDRKDQGGYTMHQDQEGDTD AGLKESPLQTPTEDGSEEPG SETSDAKSTPTAEDVTAPLV DEGAPGKQAAAQPHTEIPEG TTAEEAGIGDTPSLEDEAAG HVTQARMVSKSKDGTGSDDK KAKGADGKTKIATPRGAAPP GQKGQANATRIPAKTPPAPK TPPSSGEPPKSGDRSGYSSP GSPGTPGSRSRTPSLPTPPT REPKKVAVVRTPPKSPSSA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	437
15N chemical shifts	205
1H chemical shifts	205

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Tau (1-239)	1

Entities:

Entity 1, Tau (1-239) 239 residues - Formula weight is not available

1

MET

ALA

GLU

PRO

ARG

GLN

GLU

PHE

GLU

VAL

2

MET

GLU

ASP

HIS

ALA

GLY

THR

TYR

GLY

LEU

3

GLY

ASP

ARG

LYS

ASP

GLN

GLY

TYR

THR

4

MET

HIS

GLN

ASP

GLN

GLU

GLY

ASP

THR

ASP

5

ALA

GLY

LEU

LYS

GLU

SER

PRO

LEU

GLN

THR

6

PRO

THR

GLU

ASP

GLY

SER

GLU

PRO

GLY

7

SER

GLU

THR

SER

ASP

ALA

LYS

SER

THR

PRO

8

THR

ALA

GLU

ASP

VAL

THR

ALA

PRO

LEU

VAL

9

ASP

GLU

GLY

ALA

PRO

GLY

LYS

GLN

ALA

10

ALA

GLN

PRO

HIS

THR

GLU

ILE

PRO

GLU

GLY

11

THR

ALA

GLU

ALA

GLY

ILE

GLY

ASP

12

THR

PRO

SER

LEU

GLU

ASP

GLU

ALA

GLY

13

HIS

VAL

THR

GLN

ALA

ARG

MET

VAL

SER

LYS

14

SER

LYS

ASP

GLY

THR

GLY

SER

ASP

LYS

15

LYS

ALA

LYS

GLY

ALA

ASP

GLY

LYS

THR

LYS

16

ILE

ALA

THR

PRO

ARG

GLY

ALA

PRO

17

GLY

GLN

LYS

GLY

GLN

ALA

ASN

ALA

THR

ARG

18

ILE

PRO

ALA

LYS

THR

PRO

ALA

PRO

LYS

19

THR

PRO

SER

GLY

GLU

PRO

LYS

20

SER

GLY

ASP

ARG

SER

GLY

TYR

SER

PRO

21

GLY

SER

PRO

GLY

THR

PRO

GLY

SER

ARG

SER

22

ARG

THR

PRO

SER

LEU

PRO

THR

PRO

THR

23

ARG

GLU

PRO

LYS

VAL

ALA

VAL

ARG

24

THR

PRO

LYS

SER

PRO

SER

ALA

Samples:

sample_1: Tau (1-239), [U-99% 13C; U-99% 15N], 125 uM; sodium phosphate 50 mM; sodium azide 0.01%; D2O 5%; DSS 50 uM

sample_conditions_1: ionic strength: 0.154 M; pH: 6.8; pressure: 1 atm; temperature: 278 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 HNCA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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