BMRB Entry 36180

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PDB ID: 5zpv
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36180
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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:

Solution Structure of Thioredoxin-Like Effector Protein (TRX3) from Edwardsiella tarda

Deposition date:

2018-04-16

Original release date:

2019-05-20

Authors:

Sayed, A.; Mok, Y.

Citation:

Citation: Sayed, Ahmed; Chakraborty, Smarajit; Leung, Ka Yin; Sugii, Shigeki; Mok, Yu Keung. "Trxlp, a thioredoxin-like effector from Edwardsiella piscicida inhibits cellular redox signaling and nuclear translocation of NF-kB" Int. J. Biol. Macromol. 148, 89-8101 (2020).
PubMed: 31945434

Assembly members:

Assembly members:
Thioredoxin (H-type,TRX-H), polymer, 122 residues, 13694.305 Da.

Natural source:

Natural source: Common Name: Edwardsiella tarda Taxonomy ID: 498217 Superkingdom: Bacteria Kingdom: not available Genus/species: Edwardsiella Edwardsiella tarda

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Thioredoxin (H-type,TRX-H): MHHHHHHSSGLVPRGSQAAS VEPYSDAAFTQAQASGAPVL VDVYADWCPVCKRQERELTP LFAQPAQRDLRVFKVNFDTQ KAALQQFRVSQQSTLILYRN GQEVRRSIGETSPSALSDFL TR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	188
15N chemical shifts	95
1H chemical shifts	347

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 122 residues - 13694.305 Da.

1

MET

HIS

SER

GLY

2

LEU

VAL

PRO

ARG

GLY

SER

GLN

ALA

SER

3

VAL

GLU

PRO

TYR

SER

ASP

ALA

PHE

THR

4

GLN

ALA

GLN

ALA

SER

GLY

ALA

PRO

VAL

LEU

5

VAL

ASP

VAL

TYR

ALA

ASP

TRP

CYS

PRO

VAL

6

CYS

LYS

ARG

GLN

GLU

ARG

GLU

LEU

THR

PRO

7

LEU

PHE

ALA

GLN

PRO

ALA

GLN

ARG

ASP

LEU

8

ARG

VAL

PHE

LYS

VAL

ASN

PHE

ASP

THR

GLN

9

LYS

ALA

LEU

GLN

PHE

ARG

VAL

SER

10

GLN

SER

THR

LEU

ILE

LEU

TYR

ARG

ASN

11

GLY

GLN

GLU

VAL

ARG

SER

ILE

GLY

GLU

12

THR

SER

PRO

SER

ALA

LEU

SER

ASP

PHE

LEU

13

THR

ARG

Samples:

sample_1: TRX3, [U-13C; U-15N], 0.5 mM; phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCC(CO)NH	sample_1	isotropic	sample_conditions_1
3D NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks