A method for the NMR spectroscopic structural analysis of a target protein comprising structurally analyzing, by NMR spectroscopy, a target protein whose constituent amino acids are completely replaced with stable isotope-labeled amino acids, wherein the aromatic amino acids in the target protein are selected from the group consisting of:
- A stable isotope-labeled phenylalanine represented by the following formulae (1) to (3);
- and
- A stable isotope-labeled tyrosine represented by the following formulae (5) to (8);
- and the aliphatic amino acids constituting the target protein are stable isotope-labeled aliphatic amino acids which satisfy the following requirements of labeled patterns:
- (a) In case where a methylene group carrying two hydrogen atoms is present, one of the methylene hydrogen atoms is deuterated;
- (b) In case where a prochiral gem-methyl group is present, all of the hydrogen atoms on one of the methyl groups are completely deuterated, while the hydrogen atoms on the other methyl group are partially deuterated;
- (c) In case where a methyl group other than the foregoing ones is present, all of the hydrogen atoms on the methyl group except for one hydrogen atom are deuterated or all of the hydrogen atoms on the methyl group are deuterated;
- (d) After the deuteration in the foregoing requirements (a), (b) and (c), all of the carbon atoms of hydrogen atom-carrying methylene and/or methyl groups are replaced with 13C atoms;
- and
- (e) All of the nitrogen atoms present are completely replaced with 15N atoms