eF-site ID 5onw-ABCDEFGHIJ PDB Code 5onw Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title X-Ray crystal structure of a nucleosome core particle with its DNA site-specifically crosslinked to the histone octamer and the two H2A/H2B dimers crosslinked via H2A N38C Classification DNA BINDING PROTEIN Compound DNA (147-MER) Source Xenopus laevis (African clawed frog) (H2B11_XENLA) Sequence A:  HCYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDF KTDLRFQSSAVMALQEASEAYLVALFEDTNLAAIHAKRVT IMPKDIQLARRIRGER B:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG C:  KTRSSRAGLQFPVGRVHRLLRKGCYAERVGAGAPVYLAAV LEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELN KLLGRVTIAQGGVLPNIQSVLLP D:  RRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVND VFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAK HAVSEGTKAVTKYTSA E:  HCYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDF KTDLRFQSSAVMALQEASEAYLVALFEDTNLAAIHAKRVT IMPKDIQLARRIRGE F:  RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRG VLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT LYGFGG G:  AKTRSSRAGLQFPVGRVHRLLRKGCYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPK H:  RKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFER IAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVS EGTKAVTKYTSA I:  ATCCATATCCACCTGGTCCTACTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGGAATCCAGC TGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTT TGGTAGTAGGACCAGGTGGATATXGAT J:  ATCCATATCCACCTGGTCCTACTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGGATTCCAGC TGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTT TGGTAGTAGGACCAGGTGGATATXGAT Description Functional site 1) chain I residue 70 type sequence X description binding site for residue MN I 101 source : AC1 2) chain I residue 71 type sequence G description binding site for residue MN I 101 source : AC1 3) chain I residue -59 type sequence G description binding site for residue MN I 102 source : AC2 4) chain I residue -58 type sequence G description binding site for residue MN I 102 source : AC2 5) chain I residue 48 type sequence G description binding site for residue MN I 103 source : AC3 6) chain I residue 49 type sequence G description binding site for residue MN I 103 source : AC3 7) chain I residue 61 type sequence G description binding site for residue MN I 104 source : AC4 8) chain I residue -35 type sequence G description binding site for residue MN I 105 source : AC5 9) chain I residue -34 type sequence G description binding site for residue MN I 105 source : AC5 10) chain I residue 27 type sequence G description binding site for residue MN I 106 source : AC6 11) chain I residue 64 type sequence G description binding site for residue MN I 107 source : AC7 12) chain I residue 65 type sequence G description binding site for residue MN I 107 source : AC7 13) chain I residue -2 type sequence G description binding site for residue MN I 108 source : AC8 14) chain I residue -3 type sequence G description binding site for residue MN I 108 source : AC8 15) chain I residue 4 type sequence A description binding site for residue MN I 109 source : AC9 16) chain I residue 5 type sequence G description binding site for residue MN I 109 source : AC9 17) chain J residue 70 type sequence X description binding site for residue MN J 101 source : AD1 18) chain J residue 71 type sequence G description binding site for residue MN J 101 source : AD1 19) chain J residue -58 type sequence G description binding site for residue MN J 102 source : AD2 20) chain J residue -59 type sequence G description binding site for residue MN J 102 source : AD2 21) chain J residue 48 type sequence G description binding site for residue MN J 103 source : AD3 22) chain J residue 27 type sequence G description binding site for residue MN J 104 source : AD4 23) chain J residue -3 type sequence G description binding site for residue MN J 105 source : AD5 24) chain J residue 61 type sequence G description binding site for residue MN J 106 source : AD6 25) chain J residue -35 type sequence G description binding site for residue MN J 107 source : AD7 26) chain J residue -34 type sequence G description binding site for residue MN J 107 source : AD7 27) chain J residue 4 type sequence A description binding site for residue MN J 108 source : AD8 28) chain J residue 5 type sequence G description binding site for residue MN J 108 source : AD8 29) chain J residue 59 type sequence C description binding site for residue MN J 109 source : AD9 30) chain A residue 120 type sequence M description binding site for residue CL A 201 source : AE1 31) chain A residue 121 type sequence P description binding site for residue CL A 201 source : AE1 32) chain A residue 122 type sequence K description binding site for residue CL A 201 source : AE1 33) chain C residue 44 type sequence G description binding site for residue CL C 201 source : AE2 34) chain C residue 46 type sequence G description binding site for residue CL C 201 source : AE2 35) chain C residue 47 type sequence A description binding site for residue CL C 201 source : AE2 36) chain D residue 87 type sequence T description binding site for residue CL C 201 source : AE2 37) chain D residue 88 type sequence S description binding site for residue CL C 201 source : AE2 38) chain D residue 120 type sequence S description binding site for residue MN D 201 source : AE3 39) chain D residue 45 type sequence V description binding site for residue MN E 201 source : AE4 40) chain E residue 77 type sequence D description binding site for residue MN E 201 source : AE4 41) chain E residue 121 type sequence P description binding site for residue CL E 202 source : AE5 42) chain E residue 122 type sequence K description binding site for residue CL E 202 source : AE5 43) chain G residue 44 type sequence G description binding site for residue CL G 201 source : AE6 44) chain G residue 46 type sequence G description binding site for residue CL G 201 source : AE6 45) chain G residue 47 type sequence A description binding site for residue CL G 201 source : AE6 46) chain H residue 87 type sequence T description binding site for residue CL G 201 source : AE6 47) chain H residue 88 type sequence S description binding site for residue CL G 201 source : AE6 48) chain E residue 39 type sequence H description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 49) chain E residue 41 type sequence Y description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 50) chain E residue 42 type sequence R description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 51) chain E residue 66 type sequence P description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 52) chain E residue 67 type sequence F description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 53) chain E residue 68 type sequence Q description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 54) chain E residue 69 type sequence R description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 55) chain E residue 71 type sequence V description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 56) chain E residue 72 type sequence R description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 57) chain E residue 73 type sequence E description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 58) chain E residue 74 type sequence I description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 59) chain F residue 26 type sequence I description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 60) chain I residue -39 type sequence A description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 61) chain I residue -41 type sequence G description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 62) chain I residue -40 type sequence T description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 63) chain I residue -69 type sequence A description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 64) chain I residue -70 type sequence C description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 65) chain J residue 39 type sequence T description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 66) chain J residue 41 type sequence C description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 67) chain J residue 69 type sequence T description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 68) chain J residue 71 type sequence G description binding site for Di-peptide CYS E 40 and G47 J 70 source : AE7 69) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 70) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 71) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 72) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 73) chain E residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 74) chain F residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 75) chain A residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 76) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 77) chain F residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 78) 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 79) 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 80) 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 81) 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 82) chain A residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 83) chain E residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 84) chain A residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 85) chain A residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 86) chain E residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 87) chain E residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 88) chain A residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 89) chain E residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 90) chain A residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 91) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 92) chain E residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 93) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 94) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 95) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 96) chain A residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 97) chain E residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 98) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 99) chain E residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 100) chain A residue 110 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 101) chain E residue 110 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 102) chain C residue 95 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI3 103) chain G residue 95 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI3 104) 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 105) 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 106) 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 107) chain C residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 108) chain C residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 109) chain G residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 110) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 111) chain F residue 44 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 112) chain F residue 79 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 113) chain C residue 104 type MOD_RES sequence Q description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 114) chain G residue 104 type MOD_RES sequence Q description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 115) chain F residue 20 type MOD_RES sequence K description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 116) chain G residue 118 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 117) chain F residue 31 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 118) chain F residue 91 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 119) 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 120) 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 121) 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 122) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 123) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 124) chain F residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 125) 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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