BMRB Entry 27597

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for p53TAD in complex with S100A4
Deposition date:
2018-09-04
Original release date:
2022-02-02
Authors:
F. Dudas, Erika; Bodor, Andrea; Sebak, Fanni
Citation:

Citation: Dudas, Erika; Palfy, Gyula; Menyhard, Dora; Sebak, Fanni; Ecsedi, Peter; Nyitray, Laszlo; Bodor, Andrea. "Tumor-Suppressor p53TAD1-60 Forms a Fuzzy Complex with Metastasis-Associated S100A4: Structural Insights and Dynamics by an NMR/MD Approach"  Chembiochem 21, 3087-3095 (2020).
PubMed: 32511842

Assembly members:

Assembly members:
p53_TAD, polymer, 62 residues, Formula weight is not available
S100A4, polymer, 104 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: not known

Data sets:
Data typeCount
13C chemical shifts110
15N chemical shifts46
1H chemical shifts236

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p53TAD1
2S100A4, chain 12
3S100A4, chain 22

Entities:

Entity 1, p53TAD 62 residues - Formula weight is not available

Residues -1-0 represent a non-native affinity tag

1   GLYSERMETGLUGLUPROGLNSERASPPRO
2   SERVALGLUPROPROLEUSERGLNGLUTHR
3   PHESERASPLEUTRPLYSLEULEUPROGLU
4   ASNASNVALLEUSERPROLEUPROSERGLN
5   ALAMETASPASPLEUMETLEUSERPROASN
6   ASNILEGLUGLNTRPPHETHRGLUASPPRO
7   GLYPRO

Entity 2, S100A4, chain 1 104 residues - Formula weight is not available

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

Samples:

sample_1: p53 TAD, [U-100% 13C; U-100% 15N], 0.8 mM; S100A4 1.84 mM; MES 20 mM; sodium chloride 20 mM; TCEP 10 mM; calcium chloride 10 mM; sodium azide 3 mM; D2O, [U-2H], 50 uL; DSS 5 uL; H2O 635 uL

sample_conditions_1: ionic strength: 30 mM; pH: 5.78; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

SPARKY, Goddard - chemical shift assignment

CARA, Keller and Wuthrich - chemical shift assignment

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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