3.5.4.5	tetramer	-	-, 209661, 209665, 209666, 209668, 209669, 654638, 718695	
3.5.4.5	monomer	1 * 54000	-, 209644	
3.5.4.5	dimer	2 * 18000, SDS-PAGE	-, 650635	
3.5.4.5	dimer	2 * 31540	-, 209664, 209667	
3.5.4.5	dimer	2 * 31600, SDS-PAGE	209669	
3.5.4.5	dimer	2 * 32000, homodimer, SDS-PAGE	-, 209665, 209668	
3.5.4.5	dimer	2 * 33000, SDS-PAGE	-, 209655, 209658, 209660	
3.5.4.5	dimer	2 * 34000, SDS-PAGE	-, 209660	
3.5.4.5	dimer	2 * 35000, SDS-PAGE	-, 209653	
3.5.4.5	tetramer	4 * 13500, SDS-PAGE	209661	
3.5.4.5	tetramer	4 * 13900, SDS-PAGE	-, 755377	
3.5.4.5	homotetramer	4 * 13938, electrospray ionization mass spectrometry	-, 712889	
3.5.4.5	tetramer	4 * 14000, deduced from cdd structural gene nucleotide sequence and mini-cell experiments	209660	
3.5.4.5	homotetramer	4 * 14000, SDS-PAGE	-, 712721, 712889	
3.5.4.5	homotetramer	4 * 14072, calculated from amino acid sequence	-, 712889	
3.5.4.5	tetramer	4 * 14237, calculation from nucleotide sequence	657220	
3.5.4.5	tetramer	4 * 14600, calculation from nucleotide sequence	657220	
3.5.4.5	tetramer	4 * 14800	209667	
3.5.4.5	tetramer	4 * 15000	209668	
3.5.4.5	tetramer	4 * 15000, SDS-PAGE	657220, 670747	
3.5.4.5	tetramer	4 * 15000, SDS-PAGE, purified enzyme, homotetramer	209665	
3.5.4.5	tetramer	4 * 16000, amino acid sequence	209665	
3.5.4.5	homotetramer	4 * 16600, calculated from amino acid sequence	711824	
3.5.4.5	homotetramer	4 * 20000, SDS-PAGE	711824	
3.5.4.5	dimer	crystallization data, in the dimeric interface, residues Gly94, Ala95, Gln98, Thr100, Gly130, His131, Arg133, Gln134, Pro162, Asp163, Ala200, Asn234, Thr263 and Ile271 participate in hydrogen bonding or salt bridges	-, 752690	
3.5.4.5	tetramer	homotetramer	667736	
3.5.4.5	tetramer	homotetramer, residue Y33 is involved in enzyme folding, enzyme structure analysis using circular dichroism, molecular modeling, overview	689935	
3.5.4.5	additional information	wild-type tetramer dissociates into enzymatically inactive monomers, without intermediate forms via a non-cooperative transition. Extensive dialysis or dilution of the inativated mponomers restores completely the activity	657227	
3.5.4.5	?	x * 20800, SDS-PAGE	734018