1H, 15N, 13C Chemical Shifts of Recombinant Rat Ferrocytochrome b5, A conformation

The 15N and 13C referencing was done using the indirect referencing
according to the article
Wishart and Sykes, (1994), J. Biomol. NMR 4, 171-180

Dangi, B., Sarma, S., Yan, C., Banville, D., Guiles, R.D., "The Origin
of Difference in the Physical Properties of the Equilibrium Forms of
Cytochrome b5 Revealed Through High Resolution NMR Structures and Backbone
Dynamic Analyses," Biochemistry 37, 8289-8302 (1998).

The origin of differences in the physical properties of the equilibrium forms of cytochrome b5 revealed through high-resolution NMR structures and backbone dynamic analyses.

A simple technique for identifying protein secondary structures through the
analysis of backbone 13C chemical shifts is described. It is based on the
Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which
was originally developed for the analysis of 1H(alpha) chemical shifts. By
extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and
carbonyl 13C chemical shifts, it is now possible to use four independent
chemical-shift measurements to identify and locate protein secondary
structures. It is shown that by combining both 1H and 13C chemical-shift
indices to produce a 'consensus' estimate of secondary structure, it is
possible to achieve a predictive accuracy in excess of 92%. This suggests that
the secondary structure of peptides and proteins can be accurately obtained
from 1H and 13C chemical shifts, without recourse to NOE measurements.

Wishart and Sykes, (1994), J.B. NMR, 4 171-18
The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.

Solution Structure Of Reduced Microsomal Rat Cytochrome B5, Nmr, Minimized Average Structure

The Solution Nmr Structure Of Oxidized Rat Microsomal Cytochrome B5, Minimized Average Structure

The Solution Structure Of Oxidized Rat Microsomal Cytochrome B5, Nmr, 19 Structures

Rat Ferrocytochrome B5 A Conformation, Nmr, 1 Structure

Rat Ferrocytochrome B5 B Conformation, Nmr, 1 Structure

The Solution Nmr Structure Of The B Form Of Oxidized Rat Microsomal Cytochrome B5, Minimized Average Structure

Solution Structure Of Oxidized Rat Microsomal Cytochrome B5 In The Presence Of 2 M Guanidinium Chloride: Monitoring The Early S

Solution Structure Of The Water-Soluble Fragment Of Rat Hepatic Apocytochrome B5

Solution Structure Of F35y Mutant Of Rat Ferro Cytochrome B5, A Conformation, Ensemble Of 20 Structures

Apocytochrome B5, Ph 6.2, 298 K, Nmr, Minimized Average Structure

Apocytochrome B5, Ph 6.2, 298 K, Nmr, 10 Structures

Solution Structure Of A67v Mutant Of Rat Ferro Cytochrome B5

Dimethyl Propionate Ester Heme-Containing Cytochrome B5

The Solution Structure Of Oxidized Rat Microsomal Cytochrome B5, Nmr, 21 Structures

cytochrome b5 precursor [Rattus norvegicus]

flavocytochrome b5 chimeric protein [synthetic construct]

cytochrome b5, partial [synthetic construct]

NADH:cytochrome c reductase [synthetic construct]

cytochrome b5-like [Mesocricetus auratus]

PREDICTED: cytochrome b5 [Cricetulus griseus]

PREDICTED: cytochrome b5 [Microtus ochrogaster]

1H, 13C, and 15N chemical shifts for Rat Ferrocytochrome b5, B conformation

4mM 15N, 13C labeled in 100 mM phosphate pH 7.0