eF-site ID 1kx5-ABCDEFGH PDB Code 1kx5 Chain A, B, C, D, E, F, G, H 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 null (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 Description Functional site 1) chain D residue 45 type sequence V description BINDING SITE FOR RESIDUE MN E 3132 source : AC2 2) chain E residue 77 type sequence D description BINDING SITE FOR RESIDUE MN E 3132 source : AC2 3) chain G residue 44 type sequence G description BINDING SITE FOR RESIDUE CL H 3145 source : BC6 4) chain G residue 46 type sequence G description BINDING SITE FOR RESIDUE CL H 3145 source : BC6 5) chain G residue 47 type sequence A description BINDING SITE FOR RESIDUE CL H 3145 source : BC6 6) chain H residue 87 type sequence T description BINDING SITE FOR RESIDUE CL H 3145 source : BC6 7) chain H residue 88 type sequence S description BINDING SITE FOR RESIDUE CL H 3145 source : BC6 8) chain C residue 44 type sequence G description BINDING SITE FOR RESIDUE CL D 3146 source : BC7 9) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE CL D 3146 source : BC7 10) chain C residue 47 type sequence A description BINDING SITE FOR RESIDUE CL D 3146 source : BC7 11) chain D residue 87 type sequence T description BINDING SITE FOR RESIDUE CL D 3146 source : BC7 12) chain D residue 88 type sequence S description BINDING SITE FOR RESIDUE CL D 3146 source : BC7 13) chain A residue 121 type sequence P description BINDING SITE FOR RESIDUE CL A 3147 source : BC8 14) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE CL A 3147 source : BC8 15) chain E residue 121 type sequence P description BINDING SITE FOR RESIDUE CL E 3148 source : BC9 16) chain E residue 122 type sequence K description BINDING SITE FOR RESIDUE CL E 3148 source : BC9 17) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 18) chain A residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 19) chain E residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 20) chain A residue 116 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 21) chain E residue 116 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 22) chain A residue 123 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 23) chain E residue 123 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 24) chain A residue 111 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 25) chain E residue 111 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 26) chain D residue 3 type MOD_RES sequence S description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 27) chain D residue 10 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 28) chain D residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 29) chain D residue 18 type MOD_RES sequence T description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 30) chain H residue 3 type MOD_RES sequence S description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 31) chain H residue 10 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 32) chain H residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 33) chain H residue 18 type MOD_RES sequence T description N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI1 34) chain D residue 12 type MOD_RES sequence K description Phosphoserine => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI2 35) chain H residue 12 type MOD_RES sequence K description Phosphoserine => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI2 36) chain D residue 110 type CARBOHYD sequence E description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 37) chain H residue 110 type CARBOHYD sequence E description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 38) chain G residue 10 type CARBOHYD sequence T description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 39) chain G residue 96 type CARBOHYD sequence L description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 40) 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 41) 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 42) 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 43) chain E residue 19 type MOD_RES sequence Q description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 44) chain E residue 65 type MOD_RES sequence L description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 45) chain C residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 46) chain C residue 76 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 47) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 48) chain G residue 76 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 49) chain F residue 9 type MOD_RES sequence G description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 50) chain F residue 17 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 51) chain F residue 45 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 52) chain F residue 80 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 53) chain C residue 105 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 54) chain G residue 105 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 55) chain F residue 13 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 56) chain F residue 21 type MOD_RES sequence V description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 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 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 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) chain B residue 52 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 69) chain B residue 89 type MOD_RES sequence A description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 70) chain F residue 52 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 71) chain F residue 89 type MOD_RES sequence A description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 72) chain E residue 7 type MOD_RES sequence A description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 73) chain E residue 12 type MOD_RES sequence G description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 74) chain B residue 60 type MOD_RES sequence V description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 75) chain F residue 60 type MOD_RES sequence V description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 76) chain B residue 78 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 77) chain F residue 78 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 78) 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 79) 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 80) 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 81) 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 82) 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 83) chain A residue 38 type MOD_RES sequence P description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI14 84) chain E residue 38 type MOD_RES sequence P description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI14 85) chain A residue 42 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI15 86) chain E residue 42 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI15 87) chain A residue 58 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 88) chain E residue 58 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 89) chain E residue 81 type MOD_RES sequence D description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 90) chain E residue 108 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 91) chain A residue 81 type MOD_RES sequence D description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 92) chain A residue 108 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 93) chain A residue 14-20 type prosite sequence KAPRKQL description HISTONE_H3_1 Histone H3 signature 1. KAPRKQL source prosite : PS00322 94) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 95) chain B residue 14-18 type prosite sequence GAKRH description HISTONE_H4 Histone H4 signature. GAKRH source prosite : PS00047 96) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357

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