BMRB Entry 27549

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for TDP-43 RRM2 at 6M urea
Deposition date:
2018-07-17
Original release date:
2018-11-15
Authors:
Mackness, Brian; Morgan, Brittany; Deveau, Laura; Kathuria, Sagar; Tavella, Davide; Massi, Francesca; Zitzewitz, Jill
Citation:

Citation: Tavella, Davide; Zitzewitz, Jill; Massi, Francesca. "Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis."  Biophys. J. 115, 1673-1680 (2018).
PubMed: 30309612

Assembly members:

Assembly members:
TDP-43_RRM2, polymer, 76 residues, 8506.6182 Da.

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: pGEX-6p1

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts119
15N chemical shifts68
1H chemical shifts68

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TDP-43 RRM21

Entities:

Entity 1, TDP-43 RRM2 76 residues - 8506.6182 Da.

The first two residues (GP) are left after cleavege by PreScission protease. The following three residues (LGS) are required for cloning.

1   GLYPROLEUGLYSERARGLYSVALPHEVAL
2   GLYARGCYSTHRGLUASPMETTHRGLUASP
3   GLULEUARGGLUPHEPHESERGLNTYRGLY
4   ASPVALMETASPVALPHEILEPROLYSPRO
5   PHEARGALAPHEALAPHEVALTHRPHEALA
6   ASPASPGLNILEALAGLNSERLEUCYSGLY
7   GLUASPLEUILEILELYSGLYILESERVAL
8   HISILESERASNALAGLU

Samples:

sample_1: MOPS 20 mM; potassium chloride 25 mM; beta-mercaptoethanol 1 mM; TDP-43 RRM2, [U-100% 13C; U-100% 15N], .47 mM; urea 6 M

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

VNMRJ v2.2, Varian - collection

SPARKY, Goddard - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 600 MHz

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