BMRB Entry 17945

Name: NMR backbone assignment of a Tau protein fragment
Published: 2011-10-28

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17945

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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:

NMR backbone assignment of a Tau protein fragment

Deposition date:

2011-09-19

Original release date:

2011-10-28

Authors:

Verdegem, Dries; Sibille, Nathalie; Wieruzeski, Jean-Michel; Lippens, Guy; Landrieu, Isabelle; Huvent, Isabelle

Citation:

Citation: Sibille, Nathalie; Huvent, Isabelle; Fauquant, Caroline; Verdegem, Dries; Amniai, Laziza; Leroy, Arnaud; Wieruszeski, Jean-Michel; Lippens, Guy; Landrieu, Isabelle. "Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein." Proteins 80, 454-462 (2012).
PubMed: 22072628

Assembly members:

Assembly members:
TauF4, polymer, 124 residues, 13355.4 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: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TauF4: MHHHHHHSRSRTPSLPTPPT REPKKVAVVRTPPKSPSSAK SRLQTAPVPMPDLKNVKSKI GSTENLKHQPGGGKVQIINK KLDLSNVQSKCGSKDNIKHV PGGGSVQIVYKPVDLSKVTS KSGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	214
15N chemical shifts	99
1H chemical shifts	99

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Polypeptide	1

Entities:

Entity 1, Polypeptide 124 residues - 13355.4 Da.

The protein fragment is fused at his N-terminus to 6 Histidine residues for the purification This fragment of the neuronal Tau protein includes part of the proline rich domain [208-245] and part of the microtubule binding domain [245-324]

1

MET

HIS

SER

ARG

SER

2

ARG

THR

PRO

SER

LEU

PRO

THR

PRO

THR

3

ARG

GLU

PRO

LYS

VAL

ALA

VAL

ARG

4

THR

PRO

LYS

SER

PRO

SER

ALA

LYS

5

SER

ARG

LEU

GLN

THR

ALA

PRO

VAL

PRO

MET

6

PRO

ASP

LEU

LYS

ASN

VAL

LYS

SER

LYS

ILE

7

GLY

SER

THR

GLU

ASN

LEU

LYS

HIS

GLN

PRO

8

GLY

LYS

VAL

GLN

ILE

ASN

LYS

9

LYS

LEU

ASP

LEU

SER

ASN

VAL

GLN

SER

LYS

10

CYS

GLY

SER

LYS

ASP

ASN

ILE

LYS

HIS

VAL

11

PRO

GLY

SER

VAL

GLN

ILE

VAL

TYR

12

LYS

PRO

VAL

ASP

LEU

SER

LYS

VAL

THR

SER

13

LYS

SER

GLY

SER

Samples:

sample_1: TauF4, [U-95% 15N], 300-450 uM

Sample_2: TauF4, [U-95% 13C; U-95% 15N], 300-450 uM

sample_conditions_1: ionic strength: 25 mM; pH: 6.6; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	Sample_2	isotropic	sample_conditions_1
3D HNCACB	Sample_2	isotropic	sample_conditions_1
3D HNCO	Sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	Sample_2	isotropic	sample_conditions_1
HN(CA)N	Sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - chemical shift calculation, processing

NMRPy, In house - chemical shift assignment

NMR spectrometers:

Bruker DMX 600 MHz

BMRB	17920 19253
EMBL	CAA32636
GB	AAC04277 AAC04279 AAF97596 AAI14949 AAQ92319
REF	NP_001009068 NP_001104271 NP_001116538 NP_001116539 NP_005901
SP	P10636 P57786 Q5S6V2 Q5YCV9 Q5YCW0
TPE	CAG26750
AlphaFold	P10636 P57786 Q5S6V2 Q5YCV9 Q5YCW0