eF-site ID 1m1a-ABCDEFGH PDB Code 1m1a Chain A, B, C, D, E, F, G, H click to enlarge Title LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA Classification STRUCTURAL PROTEIN/DNA Compound Palindromic 146 Base Pair DNA Fragment Source Xenopus laevis (African clawed frog) (A0A8J0U496_XENLA) Sequence A:  KPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ DFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKR VTIMPKDIQLARRIRGERA B:  RDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFL ENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPK D:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSA E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA F:  LGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGL IYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYA LKRQGRTLYGFGG G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKK H:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSA Description Functional site 1) chain D residue 1245 type sequence V description BINDING SITE FOR RESIDUE MN E 301 source : AC1 2) chain E residue 677 type sequence D description BINDING SITE FOR RESIDUE MN E 301 source : AC1 3) chain C residue 821-827 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 4) chain D residue 1289-1311 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 5) chain A residue 466-474 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 6) chain F residue 216-220 type DNA_BIND sequence KRHRK description source Swiss-Prot : SWS_FT_FI1 7) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 8) chain F residue 259 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 9) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 10) chain F residue 277 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 11) chain B residue 31 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI12 12) chain F residue 231 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI12 13) chain A residue 456 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 14) chain B residue 91 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 15) chain E residue 656 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 16) chain F residue 291 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 17) chain A residue 457 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI14 18) chain E residue 657 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI14 19) chain A residue 480 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI15 20) chain E residue 680 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI15 21) chain A residue 515 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI16 22) chain E residue 715 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI16 23) chain A residue 522 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI17 24) chain E residue 722 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI17 25) chain G residue 1095 type MOD_RES sequence K description Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI3 26) chain H residue 1517 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI4 27) chain B residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 28) chain B residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 29) chain F residue 216 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 30) chain F residue 244 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 31) chain F residue 279 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 32) chain F residue 212 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 33) chain F residue 220 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 34) chain B residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 35) chain B residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 36) chain F residue 231 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 37) chain F residue 291 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 38) chain B residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 39) chain F residue 247 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 40) chain C residue 815 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 41) chain G residue 1015 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 42) chain G residue 1119 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 43) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 44) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 45) chain F residue 251 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 46) chain F residue 288 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9

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