Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53259

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Name: Trypanosoma brucei Tryparedoxin W39A mutant, reduced form
Published: 2026-04-23

Title:

Trypanosoma brucei Tryparedoxin W39A mutant, reduced form

Deposition date:

2025-07-05

Original release date:

2026-04-23

Authors:

Schwegler, Eric; Wagner, Annika; Hellmich, Ute

Citation:

Citation: Schwegler, Eric; Harder, Jean-Martin; Preuss, Marco; Guhl, Charlotte; Zhang, Shuaibing; Wagner, Annika; Bader, Nicole; Stallforth, Pierre; Lakemeyer, Markus; Schindelin, Hermann; Opatz, Till; Hellmich, Ute. "Inhibitor fluorination pattern tunes chemically induced protein dimerization" .

Assembly members:

Assembly members:
entity_1, polymer, 147 residues, 15961.06 Da.

Natural source:

Natural source: Common Name: Trypanosoma brucei Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGSGLAKYLPGATNLLSK SGEVSLGSLVGKTVFLYFSA SACPPCRGFTPVLAEFYEKH HVAKNFEVVLISWDENESDF HDYYGKMPWLALPFDQRSTV SELGKTFGVESIPTLITINA DTGAIIGTQARTRVIEDPDG ANFPWPN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	144
15N chemical shifts	138
1H chemical shifts	138

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 - 15961.06 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

GLY

ALA

THR

ASN

LEU

SER

LYS

3

SER

GLY

GLU

VAL

SER

LEU

GLY

SER

LEU

VAL

4

GLY

LYS

THR

VAL

PHE

LEU

TYR

PHE

SER

ALA

5

SER

ALA

CYS

PRO

CYS

ARG

GLY

PHE

THR

6

PRO

VAL

LEU

ALA

GLU

PHE

TYR

GLU

LYS

HIS

7

HIS

VAL

ALA

LYS

ASN

PHE

GLU

VAL

LEU

8

ILE

SER

TRP

ASP

GLU

ASN

GLU

SER

ASP

PHE

9

HIS

ASP

TYR

GLY

LYS

MET

PRO

TRP

LEU

10

ALA

LEU

PRO

PHE

ASP

GLN

ARG

SER

THR

VAL

11

SER

GLU

LEU

GLY

LYS

THR

PHE

GLY

VAL

GLU

12

SER

ILE

PRO

THR

LEU

ILE

THR

ILE

ASN

ALA

13

ASP

THR

GLY

ALA

ILE

GLY

THR

GLN

ALA

14

ARG

THR

ARG

VAL

ILE

GLU

ASP

PRO

ASP

GLY

15

ALA

ASN

PHE

PRO

TRP

PRO

ASN

Samples:

sample_1: Tryparedoxin, [U-13C; U-15N], 600 uM; TCEP 4 mM; sodium phosphate 25 mM; sodium chloride 150 mM; DSS 100 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

BMRB Entry 53259