BMRB Entry 27263

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the actin-binding domain of the TARP protein from Chlamydia.
Published: 2018-01-31

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27263

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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 1H, 13C, and 15N Chemical Shift Assignments for the actin-binding domain of the TARP protein from Chlamydia.

Deposition date:

2017-09-24

Original release date:

2018-01-31

Authors:

Tolchard, James; Walpole, Samuel; Miles, Andrew; Maytum, Robin; Eaglen, Lawrence; Hackstadt, Ted; Wallace, Bonnie; Blumenschein, Tharin

Citation:

Citation: Tolchard, James; Walpole, Samuel; Miles, Andrew; Maytum, Robin; Eaglen, Lawrence; Hackstadt, Ted; Wallace, Bonnie; Blumenschein, Tharin. "The intrinsically disordered Tarp protein from chlamydia binds actin with a partially preformed helix" Sci. Rep. 8, 1960-1960 (2018).
PubMed: 29386631

Assembly members:

Assembly members:
Translocated_actin-recruiting_phosphoprotein, polymer, 105 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Chlamydia trachomatis Taxonomy ID: 813 Superkingdom: Bacteria Kingdom: not available Genus/species: Chlamydia trachomatis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6P-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Translocated_actin-recruiting_phosphoprotein: GPLGSDDSGSVSSSESDKNA SVGNDGPAMKDILSAVRKHL DVVYPGDNGGSTEGPLQANQ TLGDIVQDMETTGTSQETVV SPWKGSTSSTGSAGGSGSVQ TLLPS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	236
15N chemical shifts	78
1H chemical shifts	78

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Translocated actin-recruiting phosphoprotein	1

Entities:

Entity 1, Translocated actin-recruiting phosphoprotein 105 residues - Formula weight is not available

Residues 1-5 represent remnants of the GST cleavage site.

1

GLY

PRO

LEU

GLY

SER

ASP

SER

GLY

SER

2

VAL

SER

GLU

SER

ASP

LYS

ASN

ALA

3

SER

VAL

GLY

ASN

ASP

GLY

PRO

ALA

MET

LYS

4

ASP

ILE

LEU

SER

ALA

VAL

ARG

LYS

HIS

LEU

5

ASP

VAL

TYR

PRO

GLY

ASP

ASN

GLY

6

SER

THR

GLU

GLY

PRO

LEU

GLN

ALA

ASN

GLN

7

THR

LEU

GLY

ASP

ILE

VAL

GLN

ASP

MET

GLU

8

THR

GLY

THR

SER

GLN

GLU

THR

VAL

9

SER

PRO

TRP

LYS

GLY

SER

THR

SER

THR

10

GLY

SER

ALA

GLY

SER

GLY

SER

VAL

GLN

11

THR

LEU

PRO

SER

Samples:

sample_1: Translocated actin-recruiting phosphoprotein, [U-100% 13C; U-100% 15N], 1 mM; TRIS 2 mM; DSS 200 uM; sodium azide 0.03 % w/v; D2O 10 % v/v; Calcium Chloride 0.2 mM

sample_conditions_1: ionic strength: 0.2 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNN	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNMR_Analysis v2, CCPN - chemical shift assignment

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