eF-site ID 1kx3-ABCDEFGHIJ PDB Code 1kx3 Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title X-Ray Structure of the Nucleosome Core Particle, NCP146, at 2.0 A Resolution Classification STRUCTURAL PROTEIN/DNA Compound DNA (5'(ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCTGAATTCAGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT)3') Source Xenopus laevis (African clawed frog) (1KX3) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA B:  VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF GG C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKKT D:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSAK E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA F:  KRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETR GVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGR TLYGFGG G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKK H:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSAK I:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGAATTCAGCT GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT GGTAGAATCTGCAGGTGGATATTGAT J:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGAATTCAGCT GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT GGTAGAATCTGCAGGTGGATATTGAT Description Functional site 1) chain I residue -34 type sequence G description BINDING SITE FOR RESIDUE MN I 944 source : AC1 2) chain I residue -33 type sequence G description BINDING SITE FOR RESIDUE MN I 944 source : AC1 3) chain J residue 60 type sequence G description BINDING SITE FOR RESIDUE MN J 945 source : AC2 4) chain D residue 45 type sequence V description BINDING SITE FOR RESIDUE MN E 946 source : AC3 5) chain E residue 77 type sequence D description BINDING SITE FOR RESIDUE MN E 946 source : AC3 6) chain I residue 67 type sequence T description BINDING SITE FOR RESIDUE MN J 947 source : AC4 7) chain J residue 26 type sequence G description BINDING SITE FOR RESIDUE MN J 947 source : AC4 8) chain J residue -3 type sequence G description BINDING SITE FOR RESIDUE MN J 948 source : AC5 9) chain J residue 47 type sequence G description BINDING SITE FOR RESIDUE MN J 949 source : AC6 10) chain I residue 48 type sequence G description BINDING SITE FOR RESIDUE MN I 951 source : AC8 11) chain I residue 61 type sequence G description BINDING SITE FOR RESIDUE MN I 952 source : AC9 12) chain J residue -34 type sequence G description BINDING SITE FOR RESIDUE MN J 953 source : BC1 13) chain J residue -35 type sequence G description BINDING SITE FOR RESIDUE MN J 953 source : BC1 14) chain J residue 7 type sequence G description BINDING SITE FOR RESIDUE MN J 954 source : BC2 15) chain I residue 27 type sequence G description BINDING SITE FOR RESIDUE MN I 955 source : BC3 16) chain I residue 65 type sequence G description BINDING SITE FOR RESIDUE MN I 956 source : BC4 17) chain A residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 18) chain E residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 19) chain A residue 116 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 20) chain E residue 116 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 21) chain A residue 123 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 22) chain E residue 123 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 23) chain A residue 111 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 24) chain E residue 111 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 25) chain B residue 32 type CROSSLNK sequence P description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI12 26) chain F residue 32 type CROSSLNK sequence P description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI12 27) chain A residue 42 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 28) chain E residue 42 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 29) chain A residue 57 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 30) chain A residue 80 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 31) chain E residue 57 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 32) chain E residue 80 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 33) chain A residue 58 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 34) chain E residue 58 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 35) chain A residue 81 type MOD_RES sequence D description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 36) chain A residue 108 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 37) chain E residue 81 type MOD_RES sequence D description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 38) chain E residue 108 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 39) chain D residue 110 type CARBOHYD sequence E description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 40) chain H residue 110 type CARBOHYD sequence E description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 41) chain G residue 96 type CARBOHYD sequence L description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 42) chain C residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 43) chain C residue 76 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 44) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 45) chain G residue 76 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 46) chain F residue 17 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 47) chain F residue 45 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 48) chain F residue 80 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 49) chain C residue 105 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 50) chain G residue 105 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 51) chain F residue 21 type MOD_RES sequence V description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 52) chain C residue 119 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 53) chain G residue 119 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 54) chain F residue 32 type MOD_RES sequence P description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 55) chain F residue 92 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 56) chain B residue 52 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 57) chain B residue 89 type MOD_RES sequence A description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 58) chain F residue 52 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 59) chain F residue 89 type MOD_RES sequence A description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 60) chain A residue 38 type CROSSLNK sequence P description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 61) chain B residue 92 type CROSSLNK sequence R description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 62) chain F residue 92 type CROSSLNK sequence R description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 63) chain D residue 118 type CROSSLNK sequence Y description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 64) chain G residue 37 type CROSSLNK sequence G description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 65) chain H residue 118 type CROSSLNK sequence Y description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 66) chain C residue 14 type CROSSLNK sequence A description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 67) chain F residue 48 type CROSSLNK sequence G description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 68) chain C residue 16 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 69) chain C residue 120 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 70) chain G residue 14 type CROSSLNK sequence A description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 71) chain G residue 16 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 72) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 73) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 74) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 75) chain B residue 60 type MOD_RES sequence V description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 76) chain E residue 65 type MOD_RES sequence L description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 77) chain F residue 60 type MOD_RES sequence V description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 78) chain A residue 65 type MOD_RES sequence L description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 79) chain B residue 78 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 80) chain F residue 78 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11

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