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45. bovine pancreatic trypsin inhibitor Abbreviations BPTI 

46. Minor changes are also observed at positions far removed from the sites of mutation, i.e., residues 25 and 49. These can be attributed to the variable N-terminal processing in the Aspergillus niger expression system which was used to prepare this mutant (Archer et al., unpublished work). This mutant was not available in sufficient quantity from E. coli (Chesshyre et al., 1995) for NMR spectroscopic investigation. Since the N-terminus is close to residues 25 and 49 in the tertiary structure of BPTI, it is not surprising that the additional N-terminal amino acid(s) perturb(s) the NH shifts of these residues. The additional residues were observed in the NMR spectrum, but since the major component was less than 40% of the total protein, their NH shifts have not been incorporated into Figure 4b. 

47. N.B. For the binding of elafin to HLE, K i = 2.0 × 10 - 10 M but k on = 3.6 × 10 6 M - 1 s - 1 (Ying & Simon, 1993).