eF-site ID 5dnm-ABCDEFGHIJ PDB Code 5dnm Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title Nucleosome core particle containing adducts of ruthenium(II)-toluene PTA complex Classification STRUCTURAL PROTEIN/DNA Compound Histone H3.2 Source Xenopus laevis (African clawed frog) (5DNM) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGER B:  VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF GG C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKK D:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA VSEGTKAVTKYTSAK E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGER F:  KRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETR GVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGR TLYGFGG G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKK H:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA VSEGTKAVTKYTSAK I:  ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGAATCAGCTG AACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTG GTAGTATCTGCAGGTGGATATTGAT J:  ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGATTCAGCTG AACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTG GTAGTATCTGCAGGTGGATATTGAT Description Functional site 1) chain C residue 44 type sequence G description binding site for residue SO4 D 1101 source : AC1 2) chain C residue 45 type sequence A description binding site for residue SO4 D 1101 source : AC1 3) chain C residue 46 type sequence G description binding site for residue SO4 D 1101 source : AC1 4) chain C residue 47 type sequence A description binding site for residue SO4 D 1101 source : AC1 5) chain D residue 87 type sequence T description binding site for residue SO4 D 1101 source : AC1 6) chain D residue 88 type sequence S description binding site for residue SO4 D 1101 source : AC1 7) chain D residue 45 type sequence V description binding site for residue MG E 1001 source : AC2 8) chain E residue 77 type sequence D description binding site for residue MG E 1001 source : AC2 9) chain G residue 44 type sequence G description binding site for residue SO4 G 201 source : AC3 10) chain G residue 45 type sequence A description binding site for residue SO4 G 201 source : AC3 11) chain G residue 46 type sequence G description binding site for residue SO4 G 201 source : AC3 12) chain G residue 47 type sequence A description binding site for residue SO4 G 201 source : AC3 13) chain H residue 87 type sequence T description binding site for residue SO4 G 201 source : AC3 14) chain H residue 88 type sequence S description binding site for residue SO4 G 201 source : AC3 15) chain I residue 37 type sequence A description binding site for residue SO4 G 201 source : AC3 16) chain G residue 61 type sequence E description binding site for residue RAX G 202 source : AC4 17) chain G residue 64 type sequence E description binding site for residue RAX G 202 source : AC4 18) chain H residue 46 type sequence H description binding site for residue SO4 H 201 source : AC5 19) chain H residue 47 type sequence P description binding site for residue SO4 H 201 source : AC5 20) chain H residue 48 type sequence D description binding site for residue SO4 H 201 source : AC5 21) chain H residue 49 type sequence T description binding site for residue SO4 H 201 source : AC5 22) chain H residue 102 type sequence E description binding site for residue RAX H 202 source : AC6 23) chain H residue 106 type sequence H description binding site for residue RAX H 202 source : AC6 24) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 25) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 26) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 27) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 28) chain E residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 29) chain F residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 30) chain A residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 31) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 32) chain F residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 33) 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 34) chain F 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 35) 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 36) chain F 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 37) chain A residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 38) chain E residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 39) chain A residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 40) chain A residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 41) chain E residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 42) chain E residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 43) chain A residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 44) chain E residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 45) chain A residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 46) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 47) chain E residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 48) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 49) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 50) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 51) chain A residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 52) chain E residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 53) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 54) chain E residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 55) chain A residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 56) chain E residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 57) chain C residue 95 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI3 58) chain G residue 95 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI3 59) chain C residue 36 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI4 60) chain G residue 36 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI4 61) chain H residue 117 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI4 62) chain C residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 63) chain C residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 64) chain G residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 65) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 66) chain F residue 16 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 67) chain F residue 44 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 68) chain F residue 79 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 69) chain C residue 104 type MOD_RES sequence Q description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 70) chain G residue 104 type MOD_RES sequence Q description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 71) chain F residue 20 type MOD_RES sequence K description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 72) chain C residue 118 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 73) chain G residue 118 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 74) chain F residue 31 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 75) chain F residue 91 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 76) chain F residue 47 type CROSSLNK sequence S description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 77) chain C residue 15 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 78) chain C residue 119 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 79) chain G residue 15 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 80) chain G residue 119 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 81) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 82) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 83) chain F residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 84) chain F residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9

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