BMRB Entry 15598

Name: glutathione peroxidase-type tryparedoxin peroxidase, reduced form
Published: 2008-06-05

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15598

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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:

glutathione peroxidase-type tryparedoxin peroxidase, reduced form

Deposition date:

2007-12-18

Original release date:

2008-06-05

Authors:

Melchers, Johannes; Muhle-Goll, Claudia; Krauth-Siegel, Luise

Citation:

Citation: Melchers, Johannes; Krauth-Siegel, Luise; Muhle-Goll, Claudia. "1H, 13C, and 15N assignment of the oxidized and reduced forms of T. brucei glutathione peroxidase-type tryparedoxin peroxidase"" Biomol. NMR Assignments 2, 65-68 (2008).
PubMed: 19636927

Assembly members:

Assembly members:
Px, polymer, 167 residues, Formula weight is not available

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: pET 9D

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Px: GMGSSIFDFEVLDADHKPYN LVQHKGSPLLIYNVASKCGY TKGGYETATTLYNKYKSQGF TVLAFPSNQFGGQEPGNEEE IKEFVCTKFKAEFPIMAKIN VNGENAHPLYEYMKKTKPGI LATKAIKWNFTSFLIDRDGV PVERFSPGASVKDIEEKLIP LLGSARL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts

Data type	Count
13C chemical shifts	528
15N chemical shifts	146
1H chemical shifts	1001

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Px monomer	1

Entities:

Entity 1, Px monomer 167 residues - Formula weight is not available

1

GLY

MET

GLY

SER

ILE

PHE

ASP

PHE

GLU

2

VAL

LEU

ASP

ALA

ASP

HIS

LYS

PRO

TYR

ASN

3

LEU

VAL

GLN

HIS

LYS

GLY

SER

PRO

LEU

4

ILE

TYR

ASN

VAL

ALA

SER

LYS

CYS

GLY

TYR

5

THR

LYS

GLY

TYR

GLU

THR

ALA

THR

6

LEU

TYR

ASN

LYS

TYR

LYS

SER

GLN

GLY

PHE

7

THR

VAL

LEU

ALA

PHE

PRO

SER

ASN

GLN

PHE

8

GLY

GLN

GLU

PRO

GLY

ASN

GLU

9

ILE

LYS

GLU

PHE

VAL

CYS

THR

LYS

PHE

LYS

10

ALA

GLU

PHE

PRO

ILE

MET

ALA

LYS

ILE

ASN

11

VAL

ASN

GLY

GLU

ASN

ALA

HIS

PRO

LEU

TYR

12

GLU

TYR

MET

LYS

THR

LYS

PRO

GLY

ILE

13

LEU

ALA

THR

LYS

ALA

ILE

LYS

TRP

ASN

PHE

14

THR

SER

PHE

LEU

ILE

ASP

ARG

ASP

GLY

VAL

15

PRO

VAL

GLU

ARG

PHE

SER

PRO

GLY

ALA

SER

16

VAL

LYS

ASP

ILE

GLU

LYS

LEU

ILE

PRO

17

LEU

GLY

SER

ALA

ARG

LEU

Samples:

sample_1: Px, [U-13C; U-15N; U-2H], 1 mM; NaPO4 50 mM; KCl 100 mM; H2O 90%; D2O 10%

sample_2: Px 1 mM; NaPO4 50 mM; KCl 100 mM; D2O 100%

sample_3: Px, [U-15N], 1 mM; NaPO4 50 mM; KCl 100 mM; H2O 90%; D2O 10%

sample_4: Px, [U-13C; U-15N], 1 mM; NaPO4 50 mM; KCl 100 mM; D2O 100%

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 297 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_4	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_4	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker DRX 900 MHz
Bruker DRX 800 MHz
Bruker DRX 600 MHz

BMRB	15597
PDB	2RM5 2RM6 3DWV
EMBL	CAC83349 CBH12136
GB	AAX69963 AAZ12179
REF	XP_011774419 XP_845738