BMRB Entry 52183

Title:
SIRT1 141-233
Deposition date:
2023-10-19
Original release date:
2024-08-28
Authors:
Krzysiak, Troy; Gronenborn, Angela
Citation:

Citation: Krzysiak, Troy; Choi, You-Jin; Kim, Yong Joon; Yang, Yunhan; DeHaven, Christopher; Thompson, Lariah; Ponticelli, Ryan; Mermigos, Mara; Thomas, Laurel; Marquez, Andrea; Sipula, Ian; Kemper, Jongsook Kim; Jurczak, Michael; Thomas, Gary; Gronenborn, Angela. "Inhibitory protein-protein interactions of the SIRT1 deacetylase are choreographed by post-translational modification"  Protein Sci. 33, e4938-e4938 (2024).
PubMed: 38533551

Assembly members:

Assembly members:
entity_1, polymer, 96 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: pET41

Data sets:
Data typeCount
13C chemical shifts71
15N chemical shifts37
1H chemical shifts37

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SIRT1 141-2331

Entities:

Entity 1, SIRT1 141-233 96 residues - Formula weight is not available

1   SERGLUPHEGLYTYRARGASPASNLEULEU
2   PHEGLYASPGLUILEILETHRASNGLYPHE
3   HISSERCYSGLUSERASPGLUGLUASPARG
4   ALASERHISALASERSERSERASPTRPTHR
5   PROARGPROARGILEGLYPROTYRTHRPHE
6   VALGLNGLNHISLEUMETILEGLYTHRASP
7   PROARGTHRILELEULYSASPLEULEUPRO
8   GLUTHRILEPROPROPROGLULEUASPASP
9   METTHRLEUTRPGLNILEVALILEASNILE
10   LEUSERGLUPROPROLYS

Samples:

sample_1: SIRt1 141-233, [U-100% 13C; U-100% 15N], 100 uM; HEPES 20 mM; NaCl 100 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - data analysis

CARA - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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