eF-site ID 1kx4-ABCDEFGH PDB Code 1kx4 Chain A, B, C, D, E, F, G, H click to enlarge Title X-Ray Structure of the Nucleosome Core Particle, NCP146b, at 2.6 A Resolution Classification STRUCTURAL PROTEIN/DNA Compound DNA (5'(ATCTCCAAATATCCCTTGCGGATCGTAGAAAAAGTGTGTCAAACTGCGCTATCAAAGGGAAACTTCAACTGAATTCAGTTGAAGTTTCCCTTTGATAGCGCAGTTTGACACACTTTTTCTACGATCCGCAAGGGATATTTGGAGAT)3') Source Bos taurus (Bovine) (1KX4) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA B:  KVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYG FGG C:  TRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVL EYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNK LLGRVTIAQGGVLPNIQSVLLPK D:  KKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFV NDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGEL AKHAVSEGTKAVTKYTSAK E:  HRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDF KTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVT IMPKDIQLARRIRGERA F:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPK H:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSAK Description Functional site 1) chain A residue 77 type sequence D description BINDING SITE FOR RESIDUE MN A 434 source : AC1 2) chain H residue 45 type sequence V description BINDING SITE FOR RESIDUE MN A 434 source : AC1 3) chain E residue 81 type sequence D description BINDING SITE FOR RESIDUE MN J 435 source : AC2 4) chain G residue 46 type sequence G description BINDING SITE FOR RESIDUE CL G 440 source : AC7 5) chain G residue 47 type sequence A description BINDING SITE FOR RESIDUE CL G 440 source : AC7 6) chain H residue 87 type sequence T description BINDING SITE FOR RESIDUE CL G 440 source : AC7 7) chain H residue 88 type sequence S description BINDING SITE FOR RESIDUE CL G 440 source : AC7 8) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE CL C 441 source : AC8 9) chain D residue 87 type sequence T description BINDING SITE FOR RESIDUE CL C 441 source : AC8 10) chain D residue 88 type sequence S description BINDING SITE FOR RESIDUE CL C 441 source : AC8 11) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE CL A 442 source : AC9 12) chain E residue 122 type sequence K description BINDING SITE FOR RESIDUE CL E 443 source : BC1 13) chain A residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 14) chain E residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 15) chain A residue 116 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 16) chain E residue 116 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 17) chain A residue 123 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 18) chain E residue 123 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 19) chain A residue 111 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 20) chain E residue 111 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 21) chain C residue 105 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 22) chain G residue 105 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 23) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 24) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 25) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 26) chain B residue 60 type MOD_RES sequence V description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 27) chain F residue 60 type MOD_RES sequence V description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 28) chain B residue 78 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 29) chain F residue 78 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 30) 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 31) 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 32) 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 33) 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 34) chain A residue 38 type MOD_RES sequence P description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI14 35) chain A residue 42 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI15 36) chain E residue 42 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI15 37) chain A residue 58 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 38) chain E residue 58 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 39) chain A residue 81 type MOD_RES sequence D description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 40) chain A residue 108 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 41) chain E residue 81 type MOD_RES sequence D description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 42) chain E residue 108 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 43) chain D residue 110 type CARBOHYD sequence E description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 44) chain H residue 110 type CARBOHYD sequence E description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 45) chain G residue 96 type CARBOHYD sequence L description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 46) 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 47) 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 48) 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 49) chain C residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 50) chain E residue 65 type MOD_RES sequence L description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 51) chain C residue 76 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 52) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 53) chain G residue 76 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 54) chain F residue 45 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 55) chain F residue 80 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 56) chain F residue 32 type MOD_RES sequence P description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 57) chain F residue 92 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 58) 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 59) 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 60) 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 61) 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 62) chain B residue 52 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 63) chain B residue 89 type MOD_RES sequence A description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 64) chain F residue 52 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 65) chain F residue 89 type MOD_RES sequence A description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9

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