BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17945

Title: NMR backbone assignment of a Tau protein fragment   PubMed: 22072628

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: 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).

Assembly members:
TauF4, polymer, 124 residues, 13355.4 Da.

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

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

Data sets:
Data typeCount
13C chemical shifts214
15N chemical shifts99
1H chemical shifts99

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Polypeptide1

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   METHISHISHISHISHISHISSERARGSER
2   ARGTHRPROSERLEUPROTHRPROPROTHR
3   ARGGLUPROLYSLYSVALALAVALVALARG
4   THRPROPROLYSSERPROSERSERALALYS
5   SERARGLEUGLNTHRALAPROVALPROMET
6   PROASPLEULYSASNVALLYSSERLYSILE
7   GLYSERTHRGLUASNLEULYSHISGLNPRO
8   GLYGLYGLYLYSVALGLNILEILEASNLYS
9   LYSLEUASPLEUSERASNVALGLNSERLYS
10   CYSGLYSERLYSASPASNILELYSHISVAL
11   PROGLYGLYGLYSERVALGLNILEVALTYR
12   LYSPROVALASPLEUSERLYSVALTHRSER
13   LYSSERGLYSER

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHSample_2isotropicsample_conditions_1
3D HNCACBSample_2isotropicsample_conditions_1
3D HNCOSample_2isotropicsample_conditions_1
3D HN(CO)CASample_2isotropicsample_conditions_1
HN(CA)NSample_2isotropicsample_conditions_1

Software:

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

NMRPy, In house - chemical shift assignment

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

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

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