3.5.4.5	monomer	1 * 54000	-, 209644	
3.5.4.5	dimer	2 * 35000, SDS-PAGE	-, 209653	
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	tetramer	4 * 14000, deduced from cdd structural gene nucleotide sequence and mini-cell experiments	209660	
3.5.4.5	tetramer	-	-, 209661, 209665, 209666, 209668, 209669, 654638, 718695	
3.5.4.5	tetramer	4 * 13500, SDS-PAGE	209661	
3.5.4.5	dimer	2 * 31540	-, 209664, 209667	
3.5.4.5	dimer	2 * 32000, homodimer, SDS-PAGE	-, 209665, 209668	
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	tetramer	4 * 14800	209667	
3.5.4.5	tetramer	4 * 15000	209668	
3.5.4.5	dimer	2 * 31600, SDS-PAGE	209669	
3.5.4.5	dimer	2 * 18000, SDS-PAGE	-, 650635	
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	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	tetramer	homotetramer	667736	
3.5.4.5	tetramer	4 * 15000, SDS-PAGE	657220, 670747	
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	homotetramer	4 * 16600, calculated from amino acid sequence	711824	
3.5.4.5	homotetramer	4 * 20000, SDS-PAGE	711824	
3.5.4.5	homotetramer	4 * 14000, SDS-PAGE	-, 712721, 712889	
3.5.4.5	homotetramer	4 * 13938, electrospray ionization mass spectrometry	-, 712889	
3.5.4.5	homotetramer	4 * 14072, calculated from amino acid sequence	-, 712889	
3.5.4.5	?	x * 20800, SDS-PAGE	734018	
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	4 * 13900, SDS-PAGE	-, 755377