All HN and N chemical shifts for the EGF2 domain (only) are TROSY (~ 45 Hz) shifted.

Complete NMR assignments for the second EGF domain of MIC6 from Toxoplasma gondii and re-assignment in complex with the galectin-like domain of MIC1.

Disulphide bonds are as follows: C14 - C27; C19 - C36; C38 - C54

Required for efficent assembly and correct sorting of associated protein complex

Structure Of The Mic1-GldMIC6-Egf Complex From Toxoplasma Gondii

Epidermal Growth Factor-Like Domain 2 From Toxoplasma Gondii Microneme Protein 6

The C-Terminal Domain From Micronemal Protein 1 (Mic1) From Toxoplasma Gondii

microneme protein MIC1 [Toxoplasma gondii GT1]

microneme protein MIC1 [Toxoplasma gondii ME49]

microneme protein MIC1 [Toxoplasma gondii VEG]

microneme protein MIC1 [Toxoplasma gondii p89]

microneme protein MIC1 [Toxoplasma gondii FOU]

RecName: Full=Micronemal protein 1; Flags: Precursor [Toxoplasma gondii]

The construct contains a felxible N-terminal extension which readily degraded
and was only assignable in part. The structural integrity of the EGF2 domain in
complex with MIC1 was unaffected and therefore complete assignments are
recorded.

Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for the
complex of Epidermal Growth Factor-like 2 domain from Microneme Protein 6
(Toxoplasma gondii) with the Galectin-like domain of Microneme protein 1

Swap number of residues and molecular weight of entities