THE THREE DIMENSIONAL STRUCTURE OF THE PARAMAGNETIC PROTEIN HIPIP I FROM E.HALOPHILA THROUGH NUCLEAR MAGNETIC RESONANCE
GLN 44 - ASP 45 MODEL 5 OMEGA = 148.94 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
ARG 49 - CYS 50 MODEL 8 OMEGA = 141.06 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
SER 2 - GLU 3 MODEL 9 OMEGA = 211.11 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
PRO 71 - ALA 72 MODEL 11 OMEGA = 142.48 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorhodospira halophila through nuclear magnetic resonance.
Sequence Specific Assignment of the 1H and 15N Nuclear Magnetic Resonance Spectra of the Reduced Recombinant High Potential Iron Sulfur Protein (Hipip) I from Ectothiorhodospira Halophila