BMRB Entry 53146

Name: Trypanosoma cruzi Tryparedoxin oxidized
Published: 2025-08-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53146

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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:

Trypanosoma cruzi Tryparedoxin oxidized

Deposition date:

2025-05-12

Original release date:

2025-08-19

Authors:

Schwegler, Eric; Hellmich, Ute

Citation:

Citation: Schwegler, Eric; Hellmich, Ute. "Backbone NMR assignments of the essential oxidoreductase tryparedoxin from the human pathogenic parasite Trypanosoma cruzi" Biomol. NMR Assign. 19, 267-273 (2025).
PubMed: 40719813

Assembly members:

Assembly members:
entity_1, polymer, 147 residues, 16220.47 Da.

Natural source:

Natural source: Common Name: Trypanosoma cruzi Taxonomy ID: 5693 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma cruzi

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETtrx_1b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGSGLAKYLPSTIKLVSK SGTVSPISLAGKTVFFYFSA SWCPPCRGFTPTLVEFYEKF RESKNFEVVLVTWDDEEEAY NGYFAKMPWLAIPFSSRAEL EALRSTFGVETIPTVIAVNA DTGAVVSTKGRERLLTDPEG KNFPWSD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	145
15N chemical shifts	135
1H chemical shifts	135

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Tryparedoxin	1

Entities:

Entity 1, Tryparedoxin 147 residues - 16220.47 Da.

Methionine residue 1 from the native protein sequence was replaced by residues "GAMG" (remainings of a TEV cleavage tag).

1

GLY

ALA

MET

GLY

SER

GLY

LEU

ALA

LYS

TYR

2

LEU

PRO

SER

THR

ILE

LYS

LEU

VAL

SER

LYS

3

SER

GLY

THR

VAL

SER

PRO

ILE

SER

LEU

ALA

4

GLY

LYS

THR

VAL

PHE

TYR

PHE

SER

ALA

5

SER

TRP

CYS

PRO

CYS

ARG

GLY

PHE

THR

6

PRO

THR

LEU

VAL

GLU

PHE

TYR

GLU

LYS

PHE

7

ARG

GLU

SER

LYS

ASN

PHE

GLU

VAL

LEU

8

VAL

THR

TRP

ASP

GLU

ALA

TYR

9

ASN

GLY

TYR

PHE

ALA

LYS

MET

PRO

TRP

LEU

10

ALA

ILE

PRO

PHE

SER

ARG

ALA

GLU

LEU

11

GLU

ALA

LEU

ARG

SER

THR

PHE

GLY

VAL

GLU

12

THR

ILE

PRO

THR

VAL

ILE

ALA

VAL

ASN

ALA

13

ASP

THR

GLY

ALA

VAL

SER

THR

LYS

GLY

14

ARG

GLU

ARG

LEU

THR

ASP

PRO

GLU

GLY

15

LYS

ASN

PHE

PRO

TRP

SER

ASP

Samples:

sample_1: Tryparedoxin, [U-13C; U-15N], 330 uM; hydrogenperoxide 660 uM; sodium phosphate 25 mM; sodium chloride 150 mM; DSS 150 uM

sample_conditions_1: pH: 7.5; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

CcpNMR v2 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 800 MHz