BMRB Entry 27263

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):

Data sets:
Data typeCount
13C chemical shifts236
15N chemical shifts78
1H chemical shifts78

Additional metadata:

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Assembly:

Entity Assembly IDEntity NameEntity ID
1Translocated actin-recruiting phosphoprotein1

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   GLYPROLEUGLYSERASPASPSERGLYSER
2   VALSERSERSERGLUSERASPLYSASNALA
3   SERVALGLYASNASPGLYPROALAMETLYS
4   ASPILELEUSERALAVALARGLYSHISLEU
5   ASPVALVALTYRPROGLYASPASNGLYGLY
6   SERTHRGLUGLYPROLEUGLNALAASNGLN
7   THRLEUGLYASPILEVALGLNASPMETGLU
8   THRTHRGLYTHRSERGLNGLUTHRVALVAL
9   SERPROTRPLYSGLYSERTHRSERSERTHR
10   GLYSERALAGLYGLYSERGLYSERVALGLN
11   THRLEULEUPROSER

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