BMRB Entry 52186

Title:
DBC1 52-120
Deposition date:
2023-10-20
Original release date:
2024-08-28
Authors:
Krzysiak, Troy; Kim, Yong Joon; 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, 72 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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts183
15N chemical shifts65
1H chemical shifts65

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DBC1 52-1201

Entities:

Entity 1, DBC1 52-120 72 residues - Formula weight is not available

1   SERGLUPHEGLYGLULYSGLNARGVALPHE
2   THRGLYILEVALTHRSERLEUHISASPTYR
3   PHEGLYVALVALASPGLUGLUVALPHEPHE
4   GLNLEUSERVALVALLYSGLYARGLEUPRO
5   GLNLEUGLYGLULYSVALLEUVALLYSALA
6   ALATYRASNPROGLYGLNALAVALPROTRP
7   ASNALAVALLYSVALGLNTHRLEUSERASN
8   GLNPRO

Samples:

sample_1: DBC1 52-120, [U-100% 13C; U-100% 15N], 75 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 - processing

CARA - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 900 MHz

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