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 25667

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25667
MolProbity Validation Chart

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Title: Solution Structure of the G335D Mutant of TDP-43 Amyloidogenic Core Region   PubMed: 27030292

Deposition date: 2015-06-17 Original release date: 2016-04-18

Authors: Jiang, Lei-Lei; Zhao, Jian; Hu, Hong-Yu

Citation: Jiang, Lei-Lei; Zhao, Jian; Yin, Xiao-Fang; He, Wen-Tian; Yang, Hui; Che, Mei-Xia; Hu, Hong-Yu. "Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation"  Sci. Rep. 6, 23928-23928 (2016).

Assembly members:
entity, polymer, 50 residues, 5265.847 Da.

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):
entity: MNFGAFSINPAMMAAAQAAL QSSWDMMGMLASQQNQSGPS GNNQNQGNMQ

Data sets:
Data typeCount
13C chemical shifts118
15N chemical shifts46
1H chemical shifts163

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 50 residues - 5265.847 Da.

1   METASNPHEGLYALAPHESERILEASNPRO
2   ALAMETMETALAALAALAGLNALAALALEU
3   GLNSERSERTRPASPMETMETGLYMETLEU
4   ALASERGLNGLNASNGLNSERGLYPROSER
5   GLYASNASNGLNASNGLNGLYASNMETGLN

Samples:

sample_1: GB1-TDP(311-360)-G335D, [U-99% 13C; U-99% 15N], 600 uM; sodium phosphate 20 mM; sodium chloride 50 mM; D2O, [U-99% 2H], 8%; sodium azide 0.02 w/v; H2O 92%

sample_conditions_1: ionic strength: 80 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ARIA, Linge, O'Donoghue and Nilges - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

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