BMRB Entry 52178

Name: SIRT1 1-54
Published: 2024-08-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52178

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

SIRT1 1-54

Deposition date:

2023-10-18

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, 57 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):

Entity Sequences (FASTA):
entity_1: SEFMADEAALALQPGGSPSA AGADREAASSPAGEPLRKRP RRDGPGLERSPGEPGGA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	127
15N chemical shifts	46
1H chemical shifts	46

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SIRT1 1-54	1

Entities:

Entity 1, SIRT1 1-54 57 residues - Formula weight is not available

1

SER

GLU

PHE

MET

ALA

ASP

GLU

ALA

LEU

2

ALA

LEU

GLN

PRO

GLY

SER

PRO

SER

ALA

3

ALA

GLY

ALA

ASP

ARG

GLU

ALA

SER

4

PRO

ALA

GLY

GLU

PRO

LEU

ARG

LYS

ARG

PRO

5

ARG

ASP

GLY

PRO

GLY

LEU

GLU

ARG

SER

6

PRO

GLY

GLU

PRO

GLY

ALA

Samples:

sample_1: HEPES 20 mM; NaCl 100 mM; TCEP 0.5 mM; SIRt1 1-54, [U-100% 13C; U-100% 15N], 100 uM

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCOCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

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