1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus

Journal of Biomolecular NMR

Volumn 4, Issue 2, 1994, Pages 257-278

  Remerowski, M L ^a   Domke, T ^b   Groenewegen, A ^b   Pepermans, H A M ^b   Hilbers, C W ^a   van de Ven, F J M ^a  

^a RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

^b UNILEVER RESEARCH VLAARDINGEN   (Netherlands)

Author keywords

3D NMR; Protein; Sequential assignment; Subtilisin

Indexed keywords

CARBON; HYDROGEN; MICROBIAL SERINE PROTEINASES; NITROGEN; SERINE PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; BACILLUS; CARBON ISOTOPES; COMPARATIVE STUDY; HYDROGEN; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SERINE ENDOPEPTIDASES; SUPPORT, NON-U.S. GOV'T; X-RAY DIFFRACTION;

EID: 0028399428     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/BF00175252     Document Type: Article

References (46)

1. Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts