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 26829

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for TDP-43 C-terminal domain ALS-associated variant Q331K   PubMed: 27545621

Deposition date: 2016-06-21 Original release date: 2016-08-19

Authors: Conicella, Alexander; Fawzi, Nicolas

Citation: Conicella, Alexander; Zerze, Gul; Mittal, Jeetain; Fawzi, Nicolas. "ALS Mutations Disrupt Phase Separation Mediated by alpha-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain"  Structure (Cambridge, MA, U.S.) 24, 1537-1549 (2016).

Assembly members:
Q331K_TDP-43_267-414, polymer, 151 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

Entity Sequences (FASTA):
Q331K_TDP-43_267-414: GHMNRQLERSGRFGGNPGGF GNQGGFGNSRGGGAGLGNNQ GSNMGGGMNFGAFSINPAMM AAAQAALKSSWGMMGMLASQ QNQSGPSGNNQNQGNMQREP NQAFGSGNNSYSGSNSGAAI GWGSASNAGSGSGFNGGFGS SMDSKSSGWGM

Data sets:
Data typeCount
13C chemical shifts256
15N chemical shifts136
1H chemical shifts136

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Q331K TDP-43_267-414 Monomer1

Entities:

Entity 1, Q331K TDP-43_267-414 Monomer 151 residues - Formula weight is not available

Residues 1-3 comprise the cloning artifact left after removal of the N-terminal affinity tag by cleavage with TEV protease.

1   GLYHISMETASNARGGLNLEUGLUARGSER
2   GLYARGPHEGLYGLYASNPROGLYGLYPHE
3   GLYASNGLNGLYGLYPHEGLYASNSERARG
4   GLYGLYGLYALAGLYLEUGLYASNASNGLN
5   GLYSERASNMETGLYGLYGLYMETASNPHE
6   GLYALAPHESERILEASNPROALAMETMET
7   ALAALAALAGLNALAALALEULYSSERSER
8   TRPGLYMETMETGLYMETLEUALASERGLN
9   GLNASNGLNSERGLYPROSERGLYASNASN
10   GLNASNGLNGLYASNMETGLNARGGLUPRO
11   ASNGLNALAPHEGLYSERGLYASNASNSER
12   TYRSERGLYSERASNSERGLYALAALAILE
13   GLYTRPGLYSERALASERASNALAGLYSER
14   GLYSERGLYPHEASNGLYGLYPHEGLYSER
15   SERMETASPSERLYSSERSERGLYTRPGLY
16   MET

Samples:

sample-1: Q331K TDP-43_267-414, [U-99% 13C; U-99% 15N], 20 uM; MES 20 mM

283_K: pH: 6.1; pressure: 1 atm; temperature: 283 K

298_K: pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample-1isotropic298_K
3D HNCACBsample-1isotropic298_K
3D CBCA(CO)NHsample-1isotropic298_K

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Bruker Avance 500 MHz

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