20210801 20180803 20171025 20210801 IID50308 Histone H1.11L Gallus gallus 225 P08287 Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. 0 0 N-acetylserine 2 2 H11L_CHICK H11L_CHICK MSETAPAPAAEAAPAAAPAPAKAAAKKPKKAAGGAKARKPAGPSVTELITKAVSASKERKGLSLAALKKALAAGGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFRLSKKPGEVKEKAPKKKASAAKPKKPAAKKPAAAAKKPKKAVAVKKSPKKAKKPAASATKKSAKSPKKVTKAVKPKKAVAAKSPAKAKAVKPKAAKPKAAKPKAAKAKKAAAKKK 2 1ghcA 41 114 order 1 3 115 225 disorder 2 4 115 225 disorder 3 1 1ghc NMR 7727360 C.CERF,G.LIPPENS,V.RAMAKRISHNAN,S.MUYLDERMANS,A.SEGERS,L.WYNS,S.J.WODAK,K.HALLENGA HOMO- AND HETERONUCLEAR TWO-DIMENSIONAL NMR STUDIES OF THE GLOBULAR DOMAIN OF HISTONE H1: FULL ASSIGNMENT, TERTIARY STRUCTURE, AND COMPARISON WITH THE GLOBULAR DOMAIN OF HISTONE H5. 1994 BIOCHEMISTRY 33 11079 nmr 1ghc A 41 114 100 0 1 1ghc 3620 Monomer monomer 1ghcA P08287 IID50308 2 NMR, CD 30301810 Abigail L Turner , Matthew Watson , Oscar G Wilkins , Laura Cato , Andrew Travers , Jean O Thomas, Katherine Stott Highly disordered histone H1-DNA model complexes and their condensates 2018 Proc. Natl. Acad. Sci. USA 115 11964 3 NMR, CD 30301810 Abigail L Turner , Matthew Watson , Oscar G Wilkins , Laura Cato , Andrew Travers , Jean O Thomas, Katherine Stott Highly disordered histone H1-DNA model complexes and their condensates 2018 Proc. Natl. Acad. Sci. USA 115 11964 43-114 1-42,115-225 49-102 1-48,103-225 41-48,103-113 5-43,60-75,122-225