BMRB Entry 52253

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52253

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Title:
Backbone 1H, 15N and 13C Chemical shift Assignments for TAR DNA-binding protein of 43 kDa C-terminal low-complexity
Deposition date:
2023-12-30
Original release date:
2024-01-16
Authors:
Haider, Raza; Penumutchu, Srinivasa; Boyko, Solomiia; Surewicz, Witold
Citation:

Citation: Haider, Raza; Penumutchu, Srinivasa; Boyko, Solomiia; Surewicz, Witold. "Phosphomimetic substitutions in TDP-43's transiently alpha-helical region suppress phase separation"  Biophys. J. 123, 361-373 (2024).
PubMed: 38178578

Assembly members:

Assembly members:
entity_1, polymer, 150 residues, 14708.67 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRSET-B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSNRQLERSGRFGGNPGGFG NQGGFGNSRGGGAGLGNNQG SNMGGGMNFGAFSINPAMMA AAQAALQSSWGMMGMLASQQ NQSGPSGNNQNQGNMQREPN QAFGSGNNSYSGSNSGAAIG WGSASNAGSGSGFNGGFGSS MDSKSSGWGM

Data sets:
Data typeCount
13C chemical shifts252
15N chemical shifts142
1H chemical shifts142

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1wild-type TDP-43 low complexity domain fragment1

Entities:

Entity 1, wild-type TDP-43 low complexity domain fragment 150 residues - 14708.67 Da.

1   GLYSERASNARGGLNLEUGLUARGSERGLY
2   ARGPHEGLYGLYASNPROGLYGLYPHEGLY
3   ASNGLNGLYGLYPHEGLYASNSERARGGLY
4   GLYGLYALAGLYLEUGLYASNASNGLNGLY
5   SERASNMETGLYGLYGLYMETASNPHEGLY
6   ALAPHESERILEASNPROALAMETMETALA
7   ALAALAGLNALAALALEUGLNSERSERTRP
8   GLYMETMETGLYMETLEUALASERGLNGLN
9   ASNGLNSERGLYPROSERGLYASNASNGLN
10   ASNGLNGLYASNMETGLNARGGLUPROASN
11   GLNALAPHEGLYSERGLYASNASNSERTYR
12   SERGLYSERASNSERGLYALAALAILEGLY
13   TRPGLYSERALASERASNALAGLYSERGLY
14   SERGLYPHEASNGLYGLYPHEGLYSERSER
15   METASPSERLYSSERSERGLYTRPGLYMET

Samples:

sample_1: wild-type TDP-43 low complexity domain, [U-99% 13C; U-99% 15N], 20 uM; 2-(N-morpholino)ethanesulfonic acid (MES) buffer 20 mM

sample_conditions_1: ionic strength: 0 M; pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6.2 - collection

NMRPipe v2022.311.13.21 - processing

NMRFAM-SPARKY v1.470 - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks