eF-site ID 1kx5-ABCDEFGHIJ PDB Code 1kx5 Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title X-Ray Structure of the Nucleosome Core Particle, NCP147, at 1.9 A Resolution Classification STRUCTURAL PROTEIN/DNA Compound DNA (5'(ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCTGGAATCCAGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGTATCTGCAGGTGGATATTGAT)3') Source Bos taurus (Bovine) (1KX5) Sequence A:  ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHR YRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKT DLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIM PKDIQLARRIRGERA B:  SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARR GGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKT VTAMDVVYALKRQGRTLYGFGG C:  SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYA ERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIP RHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT ESSKSKSK D:  AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYK VLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHY NKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTS AK E:  ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHR YRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKT DLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIM PKDIQLARRIRGERA F:  SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARR GGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKT VTAMDVVYALKRQGRTLYGFGG G:  SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYA ERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIP RHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT ESSKSKSK H:  AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYK VLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHY NKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTS AK I:  ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGGAATCCAGC TGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTT TGGTAGTATCTGCAGGTGGATATTGAT J:  ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGGATTCCAGC TGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTT TGGTAGTATCTGCAGGTGGATATTGAT Description Functional site 1) chain J residue 61 type sequence G description BINDING SITE FOR RESIDUE MN J 3131 source : AC1 2) chain D residue 45 type sequence V description BINDING SITE FOR RESIDUE MN E 3132 source : AC2 3) chain E residue 77 type sequence D description BINDING SITE FOR RESIDUE MN E 3132 source : AC2 4) chain J residue 27 type sequence G description BINDING SITE FOR RESIDUE MN J 3133 source : AC3 5) chain J residue -3 type sequence G description BINDING SITE FOR RESIDUE MN J 3134 source : AC4 6) chain J residue 48 type sequence G description BINDING SITE FOR RESIDUE MN J 3135 source : AC5 7) chain I residue 48 type sequence G description BINDING SITE FOR RESIDUE MN I 3137 source : AC7 8) chain I residue 61 type sequence G description BINDING SITE FOR RESIDUE MN I 3138 source : AC8 9) chain J residue -34 type sequence G description BINDING SITE FOR RESIDUE MN J 3139 source : AC9 10) chain J residue -35 type sequence G description BINDING SITE FOR RESIDUE MN J 3139 source : AC9 11) chain I residue 27 type sequence G description BINDING SITE FOR RESIDUE MN I 3140 source : BC1 12) chain I residue 5 type sequence G description BINDING SITE FOR RESIDUE MN I 3141 source : BC2 13) chain I residue -3 type sequence G description BINDING SITE FOR RESIDUE MN I 3142 source : BC3 14) chain I residue -2 type sequence G description BINDING SITE FOR RESIDUE MN I 3142 source : BC3 15) chain I residue -35 type sequence G description BINDING SITE FOR RESIDUE MN I 3143 source : BC4 16) chain I residue -34 type sequence G description BINDING SITE FOR RESIDUE MN I 3143 source : BC4 17) chain J residue 5 type sequence G description BINDING SITE FOR RESIDUE MN J 3144 source : BC5 18) chain G residue 44 type sequence G description BINDING SITE FOR RESIDUE CL H 3145 source : BC6 19) chain G residue 46 type sequence G description BINDING SITE FOR RESIDUE CL H 3145 source : BC6 20) chain G residue 47 type sequence A description BINDING SITE FOR RESIDUE CL H 3145 source : BC6 21) chain H residue 87 type sequence T description BINDING SITE FOR RESIDUE CL H 3145 source : BC6 22) chain H residue 88 type sequence S description BINDING SITE FOR RESIDUE CL H 3145 source : BC6 23) chain C residue 44 type sequence G description BINDING SITE FOR RESIDUE CL D 3146 source : BC7 24) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE CL D 3146 source : BC7 25) chain C residue 47 type sequence A description BINDING SITE FOR RESIDUE CL D 3146 source : BC7 26) chain D residue 87 type sequence T description BINDING SITE FOR RESIDUE CL D 3146 source : BC7 27) chain D residue 88 type sequence S description BINDING SITE FOR RESIDUE CL D 3146 source : BC7 28) chain A residue 121 type sequence P description BINDING SITE FOR RESIDUE CL A 3147 source : BC8 29) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE CL A 3147 source : BC8 30) chain E residue 121 type sequence P description BINDING SITE FOR RESIDUE CL E 3148 source : BC9 31) chain E residue 122 type sequence K description BINDING SITE FOR RESIDUE CL E 3148 source : BC9 32) chain A residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 33) chain E residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 34) chain A residue 116 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 35) chain E residue 116 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 36) chain A residue 123 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 37) chain E residue 123 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 38) chain A residue 111 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 39) chain E residue 111 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 40) chain B residue 78 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 41) chain F residue 78 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 42) 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 43) 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 44) chain A residue 29 type CROSSLNK sequence A description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 45) 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 46) 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 47) chain A residue 38 type MOD_RES sequence P description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI14 48) chain E residue 38 type MOD_RES sequence P description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI14 49) chain A residue 42 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI15 50) chain E residue 42 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI15 51) chain A residue 58 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 52) chain E residue 58 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 53) chain A residue 81 type MOD_RES sequence D description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 54) chain A residue 108 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 55) chain E residue 81 type MOD_RES sequence D description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 56) chain E residue 108 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 57) chain C residue 119 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 58) chain G residue 119 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 59) chain F residue 32 type MOD_RES sequence P description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 60) chain F residue 92 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 61) chain B residue 52 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 62) chain B residue 89 type MOD_RES sequence A description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 63) chain F residue 52 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 64) chain F residue 89 type MOD_RES sequence A description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) chain G 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 72) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 73) chain B residue 14-18 type prosite sequence GAKRH description HISTONE_H4 Histone H4 signature. GAKRH source prosite : PS00047 74) chain A residue 14-20 type prosite sequence KAPRKQL description HISTONE_H3_1 Histone H3 signature 1. KAPRKQL source prosite : PS00322 75) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 76) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 77) chain D residue 3 type MOD_RES sequence S description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 78) chain D residue 10 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 79) chain D residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 80) chain D residue 18 type MOD_RES sequence T description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 81) chain H residue 3 type MOD_RES sequence S description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 82) chain H residue 10 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 83) chain H residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 84) chain H residue 18 type MOD_RES sequence T description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 85) chain B residue 60 type MOD_RES sequence V description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 86) chain F residue 60 type MOD_RES sequence V description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 87) chain E residue 7 type MOD_RES sequence A description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 88) chain E residue 12 type MOD_RES sequence G description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 89) chain D residue 12 type MOD_RES sequence K description Phosphoserine => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI2 90) chain H residue 12 type MOD_RES sequence K description Phosphoserine => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI2 91) chain D residue 110 type CARBOHYD sequence E description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 92) chain H residue 110 type CARBOHYD sequence E description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 93) chain G residue 10 type CARBOHYD sequence T description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 94) chain G residue 96 type CARBOHYD sequence L description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 95) 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 96) 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 97) 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 98) chain C residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 99) chain E residue 65 type MOD_RES sequence L description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 100) chain C residue 76 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 101) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 102) chain G residue 76 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 103) chain F residue 9 type MOD_RES sequence G description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 104) chain F residue 17 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 105) chain F residue 45 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 106) chain F residue 80 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 107) chain E residue 19 type MOD_RES sequence Q description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 108) chain C residue 105 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 109) chain G residue 105 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 110) chain F residue 13 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 111) chain F residue 21 type MOD_RES sequence V description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6

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