Table 1 of Yeagle, Mol Vis 2000; 6:125-131.


Table 1. 1H chemical shifts for rhoviih

The specific 1H chemical shifts were assigned for each of the hydrogens in the peptide according to methods described in the text. H-alpha is the hydrogen attached to the alpha carbon, NH is the hydrogen attached to the amide nitrogen, H-beta are the beta hydrogens on the side chain of the amino acids and other are remaining side chain hydrogens, NH-Calpha is the coupling constant referred to in the text.

                        Coupling (Hz)
                    ---------------------
Residue   H-alpha      NH        H-beta         Other        NH-Ca
-------   -------   ---------   ---------   --------------   -----

 Pro1      4.13     2.19
 Ala2      4.3      8.55        1.15
 Phe3      4.46     7.96        2.72,2.96   7.17               5
 Phe4      4.56     8.1         2.79,3.03   7.24
 Ala5      4.33     8.14        1.25                           4
 Lys6      4.32     8.08        1.51,1.72   1.34,2.76
 Thr7      4.3      7.69        4           1.03
 Ser8      4.33     7.84        3.56,3.64
 Ala9      4.3      8.06        1.19
 Val10     4.09     7.64        1.9         0.75
 Tyr11     4.47     7.79        2.66,2.84   6.95,6.59
 Asn12     4.77     8.24        2.37,2.61   7.47,6.94
 Pro13     4.33     1.84,1.98   3.51,3.58
 Val14     3.94     7.79        1.99        0.84,0.80
 Ile15     4.05     7.5         1.68        1.30,1.04,0.72
 Tyr16     4.43     7.76        2.70,2.88   6.96,6.60
 Ile17     4.1      7.77        1.75        0.82,1.11,1.46     5
 Met18     4.3      7.95        1.81,1.91   2.43               5
 Met19     4.31     7.88        1.78,1.89   2.46
 Asn20     4.51     8.09        2.44,2.55   6.90,7.39
 Lys21     4.17     7.88        1.50,1.68   1.28,2.73
 Gln22     4.16     7.88        1.84,1.69   2.07,6.78
 Phe23     4.51     7.88        2.80,3.03   7.22
 Arg24     4.32     8.08        1.71        1.50,3.10
 Asn25     4.53     8.13        2.48,2.55                      4

Yeagle, Mol Vis 2000; 6:125-131 <http://www.molvis.org/molvis/v6/a17/>
©2000 Molecular Vision <http://www.molvis.org/molvis/>
ISSN 1090-0535