BMRB Entry 51438

Name: Deuterated chemical shifts of TcART
Published: 2022-06-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51438

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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:

Deuterated chemical shifts of TcART

Deposition date:

2022-05-13

Original release date:

2022-06-21

Authors:

Lindemann, Florian; Friedrich, Daniel; Schmieder, Peter; Oschkinat, Hartmut

Citation:

Citation: Belyy, Alexander; Lindemann, Florian; Roderer, Daniel; Funk, Johanna; Bardiaux, Benjamin; Protze, Jonas; Bieling, Peter; Oschkinat, Hartmut; Raunser, Stefan. "Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin" Nat. Commun. 13, 4202-4202 (2022).
PubMed: 35858890

Assembly members:

Assembly members:
TcART, polymer, 194 residues, 21703.8062 Da.

Natural source:

Natural source: Common Name: Photorhabdus luminescens Taxonomy ID: 29488 Superkingdom: Bacteria Kingdom: not available Genus/species: Photorhabdus luminescens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pB137

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TcART: MSTTSTNLQKKSFTLYRADN RSFEEMQSKFPEGFKAWTPL DTKMARQFASIFIGQKDTSN LPKETVKNISTWGAKPKLKD LSNYIKYTKDKSTVWVSTAI NTEAGGQSSGAPLHKIDMDL YEFAIDGQKLNPLPEGRTKN MVPSLLLDTPQIETSSIIAL NHGPVNDAEISFLTTIPLKN VKPHKRGTLEVLFQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	526
15N chemical shifts	174
1H chemical shifts	174

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TccC3	1

Entities:

Entity 1, TccC3 194 residues - 21703.8062 Da.

1

MET

SER

THR

SER

THR

ASN

LEU

GLN

LYS

2

LYS

SER

PHE

THR

LEU

TYR

ARG

ALA

ASP

ASN

3

ARG

SER

PHE

GLU

MET

GLN

SER

LYS

PHE

4

PRO

GLU

GLY

PHE

LYS

ALA

TRP

THR

PRO

LEU

5

ASP

THR

LYS

MET

ALA

ARG

GLN

PHE

ALA

SER

6

ILE

PHE

ILE

GLY

GLN

LYS

ASP

THR

SER

ASN

7

LEU

PRO

LYS

GLU

THR

VAL

LYS

ASN

ILE

SER

8

THR

TRP

GLY

ALA

LYS

PRO

LYS

LEU

LYS

ASP

9

LEU

SER

ASN

TYR

ILE

LYS

TYR

THR

LYS

ASP

10

LYS

SER

THR

VAL

TRP

VAL

SER

THR

ALA

ILE

11

ASN

THR

GLU

ALA

GLY

GLN

SER

GLY

12

ALA

PRO

LEU

HIS

LYS

ILE

ASP

MET

ASP

LEU

13

TYR

GLU

PHE

ALA

ILE

ASP

GLY

GLN

LYS

LEU

14

ASN

PRO

LEU

PRO

GLU

GLY

ARG

THR

LYS

ASN

15

MET

VAL

PRO

SER

LEU

ASP

THR

PRO

16

GLN

ILE

GLU

THR

SER

ILE

ALA

LEU

17

ASN

HIS

GLY

PRO

VAL

ASN

ASP

ALA

GLU

ILE

18

SER

PHE

LEU

THR

ILE

PRO

LEU

LYS

ASN

19

VAL

LYS

PRO

HIS

LYS

ARG

GLY

THR

LEU

GLU

20

VAL

LEU

PHE

GLN

Samples:

sample_1: TcART, [non-exchangeable-D, U-13C; U-15N], 500 uM; HEPES 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.8; pressure: 1 atm; temperature: 280 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC/HMQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
HNCOCACB (H[N[co[{CA\|ca[C]}]]])	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis v2.4 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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