Supporting Material
Supporting Material
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DOI:
10.4324/9780429244612-3
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发表时间:
2019-08
期刊:
影响因子:
--
通讯作者:
W. Freeden
中科院分区:
文献类型:
--
作者:
W. Freeden
Table S2. The H and N chemical shifts at 15C of L. casei apo DHFR and its binary and ternary complexes with trimethoprim (TMP), NADPH and folinic acid. The DHFR has an N-terminal Met residue. Red colour indicates data for residues < 4 Å from ligand and yellow indicates data for residues <10 Å from ligand. Distances for residues in the folinic acid containing complexes were estimated from the L.casei DHFR.Methotrexate structure (33). The random coil chemical shift values are sequence corrected (Schwarzinger et al., 2001). Table S3.The H and N chemical shifts at 20C of L. casei apo DHFR and its binary complex with PABG (p-aminobenzoyl-L-glutamate): ~70% of the DHFR is bound to PABG in a fast-exchange equilibrium with apo DHFR. The DHFR has no N-terminal Met residue. The residues marked with an asterisk were determined for apo-DHFR by the PABG titration.