BMRB Entry 26956

Title:
Backbone assignment of S100A4 and C-ERMAD fragment of ezrin
Deposition date:
2016-11-24
Original release date:
2017-05-23
Authors:
Palfy, Gyula; Bodor, Andrea
Citation:

Citation: Biri-Kovacs, Beata; Kiss, Bence; Vadaszi, Henrietta; Gogl, Gergo; Palfy, Gyula; Homolya, Laszlo; Bodor, Andrea; Nyitray, Laszlo. "Ezrin interacts with S100A4 via both its N- and C-terminal domains"  PLoS ONE 12, e0177489-e0177489 (2017).
PubMed: 28493957

Assembly members:

Assembly members:
S100A4d9, polymer, 95 residues, 10884.45 Da.
C-ERMAD, polymer, 74 residues, 8824.83 Da.
entity_CA, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET

Data sets:
Data typeCount
15N chemical shifts89
1H chemical shifts89

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S100A4d9, 11
2S100A4d9, 21
3C-ERMAD2
4CALCIUM ION, 13
5CALCIUM ION, 23
6CALCIUM ION, 33
7CALCIUM ION, 43

Entities:

Entity 1, S100A4d9, 1 95 residues - 10884.45 Da.

1   GLYSERHISMETALACYSPROLEUGLULYS
2   ALALEUASPVALMETVALSERTHRPHEHIS
3   LYSTYRSERGLYLYSGLUGLYASPLYSPHE
4   LYSLEUASNLYSSERGLULEULYSGLULEU
5   LEUTHRARGGLULEUPROSERPHELEUGLY
6   LYSARGTHRASPGLUALAALAPHEGLNLYS
7   LEUMETSERASNLEUASPSERASNARGASP
8   ASNGLUVALASPPHEGLNGLUTYRCYSVAL
9   PHELEUSERCYSILEALAMETMETCYSASN
10   GLUPHEPHEGLUGLY

Entity 2, C-ERMAD 74 residues - 8824.83 Da.

1   GLYSERCYSLYSARGILETHRGLUALAGLU
2   LYSASNGLUARGVALGLNARGGLNLEULEU
3   THRLEUSERSERGLULEUSERGLNALAARG
4   ASPGLUASNLYSARGTHRHISASNASPILE
5   ILEHISASNGLUASNMETARGGLNGLYARG
6   ASPLYSTYRLYSTHRLEUARGGLNILEARG
7   GLNGLYASNTHRLYSGLNARGILEASPGLU
8   PHEGLUALALEU

Entity 3, CALCIUM ION, 1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: S100A4d9, [U-100% 15N], 0.4 mM; C-ERMAD 0.6 mM; MES 20 mM; NaCl 150 mM; CaCl2 10 mM; TCEP 5 mM; NaN3 3 mM; D2O, [U-100% 2H], 50 uL; DSS 5 uL

sample_conditions_1: ionic strength: 0.17 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance III 700 MHz

Related Database Links:

UNP P26447 P15311
AlphaFold Q6ICP8 Q9NSJ4

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