BMRB Entry 52184

Name: SIRT1 109-233
Published: 2024-08-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52184

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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 109-233

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, 126 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: SGPSREPPLADNLYDEDDDD EGEEEEEAAAAAIGYRDNLL FGDEIITNGFHSCESDEEDR ASHASSSDWTPRPRIGPYTF VQQHLMIGTDPRTILKDLLP ETIPPPELDDMTLWQIVINI LSEPPK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	174
15N chemical shifts	60
1H chemical shifts	60

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SIRT1 109-233	1

Entities:

Entity 1, SIRT1 109-233 126 residues - Formula weight is not available

1

SER

GLY

PRO

SER

ARG

GLU

PRO

LEU

ALA

2

ASP

ASN

LEU

TYR

ASP

GLU

ASP

3

GLU

GLY

GLU

ALA

4

ALA

ILE

GLY

TYR

ARG

ASP

ASN

LEU

5

PHE

GLY

ASP

GLU

ILE

THR

ASN

GLY

PHE

6

HIS

SER

CYS

GLU

SER

ASP

GLU

ASP

ARG

7

ALA

SER

HIS

ALA

SER

ASP

TRP

THR

8

PRO

ARG

PRO

ARG

ILE

GLY

PRO

TYR

THR

PHE

9

VAL

GLN

HIS

LEU

MET

ILE

GLY

THR

ASP

10

PRO

ARG

THR

ILE

LEU

LYS

ASP

LEU

PRO

11

GLU

THR

ILE

PRO

GLU

LEU

ASP

12

MET

THR

LEU

TRP

GLN

ILE

VAL

ILE

ASN

ILE

13

LEU

SER

GLU

PRO

LYS

Samples:

sample_1: SIRT1 109-233, [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:

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