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 36060

Title: Solution Structure of the N-terminal Domain of TDP-43

Authors: Jiang, L.-L., L.; Xue, W.; Hu, H.-Y., H.

Citation: Jiang, L.-L., L.; Xue, W.; Hu, H.-Y., H.. "Dimerization of the N-terminal Domain of TDP-43 is Required for Its Splicing Activity"  . ., .-..

Assembly members:
entity_1, polymer, 77 residues, 8502.391 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_1: MSEYIRVTEDENDEPIEIPS EDDGTVLLSTVTAQFPGASG LRYRNPVSQSMRGVRLVEGI LHAPDAGWGNLVYVVNY

Data sets:
Data typeCount
13C chemical shifts275
15N chemical shifts78
1H chemical shifts467

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 77 residues - 8502.391 Da.

1   METSERGLUTYRILEARGVALTHRGLUASP
2   GLUASNASPGLUPROILEGLUILEPROSER
3   GLUASPASPGLYTHRVALLEULEUSERTHR
4   VALTHRALAGLNPHEPROGLYALASERGLY
5   LEUARGTYRARGASNPROVALSERGLNSER
6   METARGGLYVALARGLEUVALGLUGLYILE
7   LEUHISALAPROASPALAGLYTRPGLYASN
8   LEUVALTYRVALVALASNTYR

Samples:

sample_1: TDP(1-77)-GB1-C39/C50S, U-99% 13C; U-99% 15N, 1 mM; sodium azide 0.05 v/v; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.08 M; pH: 6.5; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

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

Molmol, Koradi, Billeter and Wuthrich - structure calculation

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

SPARKY, Goddard - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz

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