BMRB Entry 51825

Name: Solid-State NMR Assignment of Tsa1 Wild Type, a decameric Peroxiredoxin, in its reduced state
Published: 2023-04-26

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51825

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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:

Solid-State NMR Assignment of Tsa1 Wild Type, a decameric Peroxiredoxin, in its reduced state

Deposition date:

2023-02-06

Original release date:

2023-04-26

Authors:

Troussicot, Laura; Vallet, Alicia; Molin, Mikael; Burmann, Bjorn; Schanda, Paul

Citation:

Citation: Troussicot, Laura; Vallet, Alicia; Molin, Mikael; Burmann, Bjorn; Schanda, Paul. "Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR" J. Am. Chem. Soc. 145, 10700-10711 (2023).
PubMed: 37140345

Assembly members:

Assembly members:
entity_1, polymer, 196 residues, 21590 Da.

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET19b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MVAQVQKQAPTFKKTAVVDG VFDEVSLDKYKGKYVVLAFI PLAFTFVCPTEIIAFSEAAK KFEEQGAQVLFASTDSEYSL LAWTNIPRKEGGLGPINIPL LADTNHSLSRDYGVLIEEEG VALRGLFIIDPKGVIRHITI NDLPVGRNVDEALRLVEAFQ WTDKNGTVLPCNWTPGAATI KPTVEDSKEYFEAANK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	372
15N chemical shifts	129
1H chemical shifts	129

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TSA1, chain 1	1
2	TSA1, chain 2	1
3	TSA1, chain 3	1
4	TSA1, chain 4	1
5	TSA1, chain 5	1
6	TSA1, chain 6	1
7	TSA1, chain 7	1
8	TSA1, chain 8	1
9	TSA1, chain 9	1
10	TSA1, chain 10	1

Entities:

Entity 1, TSA1, chain 1 196 residues - 21590 Da.

1

MET

VAL

ALA

GLN

VAL

GLN

LYS

GLN

ALA

PRO

2

THR

PHE

LYS

THR

ALA

VAL

ASP

GLY

3

VAL

PHE

ASP

GLU

VAL

SER

LEU

ASP

LYS

TYR

4

LYS

GLY

LYS

TYR

VAL

LEU

ALA

PHE

ILE

5

PRO

LEU

ALA

PHE

THR

PHE

VAL

CYS

PRO

THR

6

GLU

ILE

ALA

PHE

SER

GLU

ALA

LYS

7

LYS

PHE

GLU

GLN

GLY

ALA

GLN

VAL

LEU

8

PHE

ALA

SER

THR

ASP

SER

GLU

TYR

SER

LEU

9

LEU

ALA

TRP

THR

ASN

ILE

PRO

ARG

LYS

GLU

10

GLY

LEU

GLY

PRO

ILE

ASN

ILE

PRO

LEU

11

LEU

ALA

ASP

THR

ASN

HIS

SER

LEU

SER

ARG

12

ASP

TYR

GLY

VAL

LEU

ILE

GLU

GLY

13

VAL

ALA

LEU

ARG

GLY

LEU

PHE

ILE

ASP

14

PRO

LYS

GLY

VAL

ILE

ARG

HIS

ILE

THR

ILE

15

ASN

ASP

LEU

PRO

VAL

GLY

ARG

ASN

VAL

ASP

16

GLU

ALA

LEU

ARG

LEU

VAL

GLU

ALA

PHE

GLN

17

TRP

THR

ASP

LYS

ASN

GLY

THR

VAL

LEU

PRO

18

CYS

ASN

TRP

THR

PRO

GLY

ALA

THR

ILE

19

LYS

PRO

THR

VAL

GLU

ASP

SER

LYS

GLU

TYR

20

PHE

GLU

ALA

ASN

LYS

Samples:

sample_1: Homodecameric_TSA1_Native, [U-13C; U-15N; U-2H], 2.1 mg; Phosphate buffer 0.05 M; DTT 0.005 M

sample_conditions_1: ionic strength: 0.05 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D hNH	sample_1	isotropic	sample_conditions_1
3D hCONH	sample_1	isotropic	sample_conditions_1
3D hCOcaNH_horror	sample_1	isotropic	sample_conditions_1
3D hCANH	sample_1	isotropic	sample_conditions_1
3D hCAcoNH_BSH-CP	sample_1	isotropic	sample_conditions_1
3D hcaCBcaNH_noD	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v3.1 - chemical shift assignment, data analysis

TOPSPIN - collection, processing

NMR spectrometers:

Bruker AVANCE III 600 MHz

UNP	P34760
AlphaFold	D6VZE6