The answer to your request isn't completely simple. That is because streptavidin, once synthesized, is proteolytically processed to a core sequence. This processing involves imprecise removal of some amino acids from both the amino and carboxy termini of the primary translation product. The result is a heterogeneous population of streptavidin molecules with subunits whose termini are approximately those of the core sequence.
The sequence of the primary translation product has been deduced from the sequence of the cloned gene. The reference for this is Agarana et al. (1986), Nucleic Acids Research, vol. 14, pp 1871-1882.
A discussion of the proteolytic processing, including a description of the core sequence, is found in Chapter 8 of volume 184 of Methods in Enzymology (Avidin-Biotin Technology; Academic Press, 1990), especially pp 85-89
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