BMRB Entry 52182

Name: SIRT1 1-124
Published: 2024-08-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52182

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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 1-124

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, 125 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: SMADEAALALQPGGSPSAAG ADREAASSPAGEPLRKRPRR DGPGLERSPGEPGGAAPERE VPAAARGCPGAAAAALWREA EAEAAAAGGEQEAQATAAAG EGDNGPGLQGPSREPPLADN LYDED

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	302
15N chemical shifts	107
1H chemical shifts	107

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SIRT1 1-124	1

Entities:

Entity 1, SIRT1 1-124 125 residues - Formula weight is not available

1

SER

MET

ALA

ASP

GLU

ALA

LEU

ALA

LEU

2

GLN

PRO

GLY

SER

PRO

SER

ALA

GLY

3

ALA

ASP

ARG

GLU

ALA

SER

PRO

ALA

4

GLY

GLU

PRO

LEU

ARG

LYS

ARG

PRO

ARG

5

ASP

GLY

PRO

GLY

LEU

GLU

ARG

SER

PRO

GLY

6

GLU

PRO

GLY

ALA

PRO

GLU

ARG

GLU

7

VAL

PRO

ALA

ARG

GLY

CYS

PRO

GLY

8

ALA

LEU

TRP

ARG

GLU

ALA

9

GLU

ALA

GLU

ALA

GLY

GLU

10

GLN

GLU

ALA

GLN

ALA

THR

ALA

GLY

11

GLU

GLY

ASP

ASN

GLY

PRO

GLY

LEU

GLN

GLY

12

PRO

SER

ARG

GLU

PRO

LEU

ALA

ASP

ASN

13

LEU

TYR

ASP

GLU

ASP

Samples:

sample_1: SIRT1 1-124, [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:

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

NMRPipe - data analysis

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