BMRB Entry 26823

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26823

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments, HNHA scalar coupling, and 15N backbone relaxation data for TDP-43 C-terminal domain wild type
Deposition date:
2016-06-20
Original release date:
2016-08-19
Authors:
Conicella, Alexander; Fawzi, Nicolas
Citation:

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).
PubMed: 27545621

Assembly members:

Assembly members:
WT_TDP-43_267-414, polymer, 151 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: pJ411

Entity Sequences (FASTA):

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

Data typeCount
13C chemical shifts660
15N chemical shifts286
1H chemical shifts292
T1 relaxation values222
T2 relaxation values259
coupling constants101
heteronuclear NOE values196

Additional metadata:

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

Assembly:

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

Entities:

Entity 1, WT 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   ALAALAALAGLNALAALALEUGLNSERSER
8   TRPGLYMETMETGLYMETLEUALASERGLN
9   GLNASNGLNSERGLYPROSERGLYASNASN
10   GLNASNGLNGLYASNMETGLNARGGLUPRO
11   ASNGLNALAPHEGLYSERGLYASNASNSER
12   TYRSERGLYSERASNSERGLYALAALAILE
13   GLYTRPGLYSERALASERASNALAGLYSER
14   GLYSERGLYPHEASNGLYGLYPHEGLYSER
15   SERMETASPSERLYSSERSERGLYTRPGLY
16   MET

Samples:

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

sample-2: WT TDP-43_267-414, [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
3D HNCOsample-1isotropic298_K
3D HN(CA)COsample-1isotropic298_K
2D 1H-15N HSQCsample-1isotropic283_K
3D HNCACBsample-1isotropic283_K
3D CBCA(CO)NHsample-1isotropic283_K
hnhagp3dsample-2isotropic283_K
hsqct1etf3gpsitc3d.nlfsample-2isotropic283_K
hsqct2etf3gpsitc3d.acsample-2isotropic283_K
hsqcnoef3gpsisample-2isotropic283_K
hsqct1etf3gpsitc3d.nlfsample-2isotropic283_K
hsqct2etf3gpsitc3d.acsample-2isotropic283_K
hsqcnoef3gpsisample-2isotropic283_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks