BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50154

Title: C-terminal domain of TDP-43 at acidic pH

Deposition date: 2020-01-09 Original release date: 2021-03-10

Authors: Mompean, Miguel

Citation: Mompean, Miguel. "Deciphering the amyloid foldome of TDP-43"  .

Assembly members:
TDP-43 267-414, polymer, 169 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: pJ411

Entity Sequences (FASTA):
TDP-43 267-414: MGSDKIHHHHHHENLYFQGH MNRQLERSGRFGGNPGGFGN QGGFGNSRGGGAGLGNNQGS NMGGGMNFGAFSINPAMMAA AQAALQSSWGMMGMLASQQN QSGPSGNNQNQGNMQREPNQ AFGSGNNSYSGSNSGAAIGW GSASNAGSGSGFNGGFGSSM DSKSSGWGM

Data sets:
Data typeCount
13C chemical shifts467
15N chemical shifts163
1H chemical shifts552

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal domain of TDP-431

Entities:

Entity 1, C-terminal domain of TDP-43 169 residues - Formula weight is not available

1   METGLYSERASPLYSILEHISHISHISHIS
2   HISHISGLUASNLEUTYRPHEGLNGLYHIS
3   METASNARGGLNLEUGLUARGSERGLYARG
4   PHEGLYGLYASNPROGLYGLYPHEGLYASN
5   GLNGLYGLYPHEGLYASNSERARGGLYGLY
6   GLYALAGLYLEUGLYASNASNGLNGLYSER
7   ASNMETGLYGLYGLYMETASNPHEGLYALA
8   PHESERILEASNPROALAMETMETALAALA
9   ALAGLNALAALALEUGLNSERSERTRPGLY
10   METMETGLYMETLEUALASERGLNGLNASN
11   GLNSERGLYPROSERGLYASNASNGLNASN
12   GLNGLYASNMETGLNARGGLUPROASNGLN
13   ALAPHEGLYSERGLYASNASNSERTYRSER
14   GLYSERASNSERGLYALAALAILEGLYTRP
15   GLYSERALASERASNALAGLYSERGLYSER
16   GLYPHEASNGLYGLYPHEGLYSERSERMET
17   ASPSERLYSSERSERGLYTRPGLYMET

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 60-120 uM

sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(NCOCA)NHsample_1isotropicsample_conditions_1
3D (H)N(COCA)NHsample_1isotropicsample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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