#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:Q8YF53	-	intact:EBI-8754687|ensemblbacteria:AAL52855	-	psi-mi:q8yf53_brume(display_long)|uniprotkb:BMEI1674(locus name)	-	psi-mi:"MI:0114"(x-ray crystallography)	Kaplan-Türköz et al. (2013)	pubmed:24076024|imex:IM-21539	taxid:224914(brume)|taxid:224914("Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)")	-	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0471"(MINT)	intact:EBI-8754680|imex:IM-21539-1	-	-	psi-mi:"MI:0499"(unspecified role)	-	psi-mi:"MI:0499"(unspecified role)	-	psi-mi:"MI:0326"(protein)	-	interpro:IPR035897|interpro:IPR000157(Toll-Interleukin receptor)|rcsb pdb:4LQC|ensemblbacteria:AAL52855(transcript)|ensemblbacteria:BMEI1674(gene)|go:"GO:0007165"(signal transduction)|go:"GO:0039506"(modulation by virus of host molecular function)|go:"GO:0042802"(identical protein binding)	-	-	comment:"The structure of BtpA was solved at 3.15 A and refined to final Rwork/Rfree values of 22%/27%. Even though crystallization drops were set-up with full-length BtpA, the crystals only contained a C-terminal portion of the protein due to N-terminal degradation. The asymmetric unit (AU) of BtpA crystals contains four chains arranged as two dimers AB and CD. Chains A and C encompass residues 100 to 275 and chains B and D are composed of residues 143 to 275 with some loops missing. As dimers AB and CD are almost identical, only chains A and B will be described in this section. Residues 100 to 133 of chain A form a long helix hereafter named alpha-tail, that packs against the TIR domains of chains A and B (Fig.1A), comprised between residues 143 to 275. The TIR domain of BtpA contains the canonical secondary structures described for TIR domains: five parallel alpha-strands (alpha-A to alpha-E) surrounded by five alpha-helices (Fig.1A)."	-	figure legend:t1 f1 f2 f3|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2013/09/04	2014/10/16	rogid:5Hzca2UDIujU3XOF2BpcZ9ez7zM224914	-	intact-crc:BDF9C4271839E287	false	-	-	1	-	psi-mi:"MI:0396"(predetermined participant)	-