BMRB Entry 50759

Name: Backbone resonance assignment of Phosphorylated C-terminal intracellular domain of Tir effector from Escherichia coli O127:H6
Published: 2024-02-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50759

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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:

Backbone resonance assignment of Phosphorylated C-terminal intracellular domain of Tir effector from Escherichia coli O127:H6

Deposition date:

2021-02-10

Original release date:

2024-02-14

Authors:

Vieira, Marta

Citation:

Citation: Vieira, Marta; Hernandez, Guillem; Zhong, Qiyun; Arbesu, Miguel; Veloso, Tiago; Gomes, Tiago; Martins, Maria; Monteiro, Hugo; Frazao, Carlos; Frankel, Gad; Zanzoni, Andreas; Cordeiro, Tiago. "The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection" Commun. Biol. 7, 179-179 (2024).
PubMed: 38351154

Assembly members:

Assembly members:
entity_1, polymer, 173 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHTP8

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPRRNQPAEQTTTTTTHTVV QQQTGGNTPAQGGTDATRAE DASLNRRDSQGSVASTHWSD SSSEVVNPYAEVGGARNSLS AHQPEEHIYDEVAADPGYSV IQNFSGSGPVTGRLIGTPGQ GIQSTYALLANSGGLRLGMG GLTSGGESAVSSVNAAPTPG PVRFVWSHPQFEK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	482
15N chemical shifts	160
1H chemical shifts	160

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	pC-Tir	1

Entities:

Entity 1, pC-Tir 173 residues - Formula weight is not available

N-Terminal: two residues (GP) from HRV-3C cleavage sequence C-Terminal: Streptag (WSHPQFEK) Phosphorylated tyrosine residues Y454, Y474, Y483 and Y511.

1

GLY

PRO

ARG

ASN

GLN

PRO

ALA

GLU

GLN

2

THR

HIS

THR

VAL

3

GLN

THR

GLY

ASN

THR

PRO

ALA

4

GLN

GLY

THR

ASP

ALA

THR

ARG

ALA

GLU

5

ASP

ALA

SER

LEU

ASN

ARG

ASP

SER

GLN

6

GLY

SER

VAL

ALA

SER

THR

HIS

TRP

SER

ASP

7

SER

GLU

VAL

ASN

PRO

PTR

ALA

8

GLU

VAL

GLY

ALA

ARG

ASN

SER

LEU

SER

9

ALA

HIS

GLN

PRO

GLU

HIS

ILE

PTR

ASP

10

GLU

VAL

ALA

ASP

PRO

GLY

PTR

SER

VAL

11

ILE

GLN

ASN

PHE

SER

GLY

SER

GLY

PRO

VAL

12

THR

GLY

ARG

LEU

ILE

GLY

THR

PRO

GLY

GLN

13

GLY

ILE

GLN

SER

THR

PTR

ALA

LEU

ALA

14

ASN

SER

GLY

LEU

ARG

LEU

GLY

MET

GLY

15

GLY

LEU

THR

SER

GLY

GLU

SER

ALA

VAL

16

SER

VAL

ASN

ALA

PRO

THR

PRO

GLY

17

PRO

VAL

ARG

PHE

VAL

TRP

SER

HIS

PRO

GLN

18

PHE

GLU

LYS

Samples:

sample_1: Phosphorylated C-Tir, [U-13C; U-15N], 991.1 uM; D2O, [U-2H], 8 % v/v; sodium chloride 150 mM; HEPES 20 mM; magnesium chloride 12 mM; Adenosine triphosphate 5.5 mM; DSS 20 uM

sample_conditions_1: ionic strength: 150 mM; pH: 6.80; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.9.1 - chemical shift assignment, data analysis

TOPSPIN - NMR data acquisition and spectra processing

NMR spectrometers:

Bruker Avance 800 MHz