title: 3D 13C/1H NMR-based assignments for side-chain resonances of Lactobacillus casei dihydrofolate reductase. Evidence for similarities between the solution and crystal structures of the enzyme.
authors.forename: A
authors.initials: A
authors.lastname: Soteriou
authors.forename: M D
authors.initials: MD
authors.lastname: Carr
authors.forename: T A
authors.initials: TA
authors.lastname: Frenkiel
authors.forename: J E
authors.initials: JE
authors.lastname: McCormick
authors.forename: C J
authors.initials: CJ
authors.lastname: Bauer
authors.forename: D
authors.initials: D
authors.lastname: Sali
authors.forename: B
authors.initials: B
authors.lastname: Birdsall
authors.forename: J
authors.initials: J
authors.lastname: Feeney
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002247:Carbon Isotopes; D003460:Crystallization; D006859:Hydrogen; D007780:Lacticaseibacillus casei / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008727:Methotrexate / Q000378:metabolism; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012996:Solutions; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry* / Q000378:metabolism
chemical_list: D002247:Carbon Isotopes; D012996:Solutions; D006859:Hydrogen; D013762:Tetrahydrofolate Dehydrogenase; D008727:Methotrexate