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 28111

Title: Backbone 1H, 13C and 15N chemical shift assignments of the N-terminal portion of ALIX-PRD   PubMed: 32917811

Deposition date: 2020-03-27 Original release date: 2020-08-31

Authors: Deshmukh, Lalit; Elias, Ruben

Citation: Elias, Ruben; Ma, Wen; Ghirlando, Rodolfo; Schwieters, Charles; Reddy, Vijay; Deshmukh, Lalit. "Proline-rich domain of human ALIX contains multiple TSG101-UEV interaction sites and forms phosphorylation-mediated reversible amyloids"  Proc. Natl. Acad. Sci. U. S. A. 117, 24274-24284 (2020).

Assembly members:
ALIX, polymer, 107 residues, Formula weight is not available

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   Vector: pet11a

Entity Sequences (FASTA):
ALIX: GDELLKDLQQSIAREPSAPS IPTPAYQSSPAGGHAPTPPT PAPRTMPPTKPQPPARPPPP VLPANRAPSATAPSPVGAGT AAPAPSQTPGSAPPPQAQGW SHPQFEK

Data sets:
Data typeCount
13C chemical shifts292
15N chemical shifts106
1H chemical shifts73

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ALIX1

Entities:

Entity 1, ALIX 107 residues - Formula weight is not available

1   GLYASPGLULEULEULYSASPLEUGLNGLN
2   SERILEALAARGGLUPROSERALAPROSER
3   ILEPROTHRPROALATYRGLNSERSERPRO
4   ALAGLYGLYHISALAPROTHRPROPROTHR
5   PROALAPROARGTHRMETPROPROTHRLYS
6   PROGLNPROPROALAARGPROPROPROPRO
7   VALLEUPROALAASNARGALAPROSERALA
8   THRALAPROSERPROVALGLYALAGLYTHR
9   ALAALAPROALAPROSERGLNTHRPROGLY
10   SERALAPROPROPROGLNALAGLNGLYTRP
11   SERHISPROGLNPHEGLULYS

Samples:

sample_1: ALIX, [U-100% 13C; U-100% 15N], 1.5 mM; D2O, [U-100% 2H], 7%; sodium phosphate 20 mM; sodium chloride 50 mM; EDTA 2 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D (HACA)N(CA)CONsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1

Software:

CCPN, CCPN - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UniProt Q8WUM4

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