BMRB Entry 27516

Title:
NMR measurements reveal the structural basis of transthyretin destabilization by pathogenic mutations
Deposition date:
2018-06-08
Original release date:
2019-01-07
Authors:
Wright, Peter; Leach, Benjamin; Zhang, Xin; Kelly, Jeffery; Dyson, Jane
Citation:

Citation: Leach, Benjamin; Zhang, Xin; Kelly, Jeffery; Dyson, Jane; Wright, Peter. "NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations"  Biochemistry 57, 4421-4430 (2018).
PubMed: 29972637

Assembly members:

Assembly members:
Transthyretin_V122I, polymer, 147 residues, Formula weight is not available

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: pET 29b+

Data sets:
Data typeCount
13C chemical shifts122
15N chemical shifts115
1H chemical shifts115

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Transthyretin1

Entities:

Entity 1, Transthyretin 147 residues - Formula weight is not available

1   METALASERHISARGLEULEULEULEUCYS
2   LEUALAGLYLEUVALPHEVALSERGLUALA
3   GLYPROTHRGLYTHRGLYGLUSERLYSCYS
4   PROLEUMETVALLYSVALLEUASPALAVAL
5   ARGGLYSERPROALAILEASNVALALAVAL
6   HISVALPHEARGLYSALAALAASPASPTHR
7   TRPGLUPROPHEALASERGLYLYSTHRSER
8   GLUSERGLYGLULEUHISGLYLEUTHRTHR
9   GLUGLUGLUPHEVALGLUGLYILETYRLYS
10   VALGLUILEASPTHRLYSSERTYRTRPLYS
11   ALALEUGLYILESERPROPHEHISGLUHIS
12   ALAGLUVALVALPHETHRALAASNASPSER
13   GLYPROARGARGTYRTHRILEALAALALEU
14   LEUSERPROTYRSERTYRSERTHRTHRALA
15   VALILETHRASNPROLYSGLU

Samples:

sample_1: sodium phosphate 10 mM; potassium chloride 100 mM; transthyretin, [U-13C; U-15N; U-2H;], 800 uM

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment, collection, processing

NMR spectrometers:

  • Bruker AMX 750 MHz

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