Sequence file: Difference between revisions
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| Line 15: | Line 15: | ||
TRP 23 | TRP 23 | ||
CYSS 24 | CYSS 24 | ||
Reduced cysteine residues are denoted by CYS, oxidized cystine residues (involved in disulfide bridges) are denoted by CYSS, if the standard residue library is used. | |||
By default, OMEGA torsion angles, e.g. in the peptide bonds in proteins, are kept fixed in the trans position, <math>\omega = 180</math>. | By default, OMEGA torsion angles, e.g. in the peptide bonds in proteins, are kept fixed in the trans position, <math>\omega = 180</math>. | ||
Revision as of 14:38, 29 January 2009
Basic format
GLY 11 SER 12 ILE 13 PRO 14 CYSS 15 LEU 16 LEU 17 SER 18 cPRO 19 TRP 20 SER 21 GLU 22 TRP 23 CYSS 24
Reduced cysteine residues are denoted by CYS, oxidized cystine residues (involved in disulfide bridges) are denoted by CYSS, if the standard residue library is used.
By default, OMEGA torsion angles, e.g. in the peptide bonds in proteins, are kept fixed in the trans position, .
Equivalent forms
Residue numbers can be omitted if they are equal to the residue number of the previous residue plus 1. The first residue number can be omitted if it is equal to 1.
GLY 11 SER ILE PRO CYSS LEU LEU SER cPRO TRP SER GLU TRP CYSS
Multiple residues can be written on a line:
GLY 11 SER ILE PRO CYSS LEU LEU SER cPRO TRP SER GLU TRP CYSS