eF-site ID 1eqz-ABCDEFGH PDB Code 1eqz Chain A, B, C, D, E, F, G, H click to enlarge Title X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.5 A RESOLUTION Classification STRUCTURAL PROTEIN/DNA Compound 146 NUCLEOTIDES LONG DNA Source ORGANISM_COMMON: chicken; ORGANISM_SCIENTIFIC: Gallus gallus; Sequence A:  SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYA ERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIP RHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKT DSHKA B:  VTKTQKKGDKKRKKSRKESYSIYVYKVLKQVHPDTGISSK AMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTA VRLLLPGELAKHAVSEGTKAVTKYTSSK C:  APATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQ RLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTN LCAIHAKRVTIMPKDIQLARRIRGERA D:  GAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEE TRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQ GRTLYGFGG E:  GRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAE RVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPR HLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTD SHKAKAK F:  TKTQKKGDKKRKKSRKESYSIYVYKVLKQVHPDTGISSKA MGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAV RLLLPGELAKHAVSEGTKAVTKYTSSK G:  PRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQ KSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEA SEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA H:  KGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRIS GLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVV YALKRQGRTLYGFGG Description Functional site 1) chain A residue 44 type sequence G description BINDING SITE FOR RESIDUE CL A 449 source : AC1 2) chain A residue 46 type sequence G description BINDING SITE FOR RESIDUE CL A 449 source : AC1 3) chain A residue 47 type sequence A description BINDING SITE FOR RESIDUE CL A 449 source : AC1 4) chain B residue 90 type sequence T description BINDING SITE FOR RESIDUE CL A 449 source : AC1 5) chain B residue 91 type sequence S description BINDING SITE FOR RESIDUE CL A 449 source : AC1 6) chain E residue 44 type sequence G description BINDING SITE FOR RESIDUE CL E 450 source : AC2 7) chain E residue 46 type sequence G description BINDING SITE FOR RESIDUE CL E 450 source : AC2 8) chain E residue 47 type sequence A description BINDING SITE FOR RESIDUE CL E 450 source : AC2 9) chain F residue 90 type sequence T description BINDING SITE FOR RESIDUE CL E 450 source : AC2 10) chain F residue 91 type sequence S description BINDING SITE FOR RESIDUE CL E 450 source : AC2 11) chain A residue 64 type sequence E description BINDING SITE FOR RESIDUE CAC G 451 source : AC3 12) chain B residue 47 type sequence Q description BINDING SITE FOR RESIDUE CAC G 451 source : AC3 13) chain B residue 48 type sequence V description BINDING SITE FOR RESIDUE CAC G 451 source : AC3 14) chain B residue 49 type sequence H description BINDING SITE FOR RESIDUE CAC G 451 source : AC3 15) chain G residue 73 type sequence E description BINDING SITE FOR RESIDUE CAC G 451 source : AC3 16) chain G residue 76 type sequence Q description BINDING SITE FOR RESIDUE CAC G 451 source : AC3 17) chain G residue 77 type sequence D description BINDING SITE FOR RESIDUE CAC G 451 source : AC3 18) chain H residue 22 type sequence L description BINDING SITE FOR RESIDUE CAC G 451 source : AC3 19) chain A residue 124 type sequence K description BINDING SITE FOR RESIDUE K J 453 source : AC5 20) chain D residue 16-20 type DNA_BIND sequence KRHRK description source Swiss-Prot : SWS_FT_FI1 21) chain H residue 16-20 type DNA_BIND sequence KRHRK description source Swiss-Prot : SWS_FT_FI1 22) chain B residue 21 type DNA_BIND sequence T description source Swiss-Prot : SWS_FT_FI1 23) chain F residue 21 type DNA_BIND sequence T description source Swiss-Prot : SWS_FT_FI1 24) chain D residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 25) chain H residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 26) chain E residue 120 type MOD_RES sequence T description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 27) chain D residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 28) chain H residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 29) chain C residue 64 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 30) chain G residue 18 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 31) chain G residue 23 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 32) chain G residue 64 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 33) chain C residue 37 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI15 34) chain G residue 37 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI15 35) chain C residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 36) chain C residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 37) chain G residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 38) chain G residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 39) chain C residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI20 40) chain G residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI20 41) chain C residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 42) chain G residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 43) chain C residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI22 44) chain G residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI22 45) chain C residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI23 46) chain G residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI23 47) chain D 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 48) chain H 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 49) chain D 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 50) chain G residue 27 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 51) chain H 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 52) chain G residue 28 type MOD_RES sequence S description Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 53) chain C residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 54) chain G residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 55) chain C residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI17 56) chain C residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI17 57) chain G residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI17 58) chain G residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI17 59) chain C residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI18 60) chain G residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI18 61) chain G residue 17 type MOD_RES sequence R description Phosphoserine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI2 62) chain E residue 10 type MOD_RES sequence A description Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI3 63) chain E residue 96 type MOD_RES sequence L description Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI3 64) chain F residue 121 type MOD_RES sequence Y description N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI4 65) chain D residue 16 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 66) chain D residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 67) chain D residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 68) chain H residue 8 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 69) chain H residue 16 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 70) chain H residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 71) chain H residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 72) chain D residue 20 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 73) chain H residue 12 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 74) chain H residue 20 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 75) chain D residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 76) chain D residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 77) chain H residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 78) chain H residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 79) chain D residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 80) chain H residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 81) chain E residue 119 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 82) chain E residue 120 type MOD_RES sequence T description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 83) chain D residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 84) chain D residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 85) chain H residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 86) chain H residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 87) chain D residue 14-18 type prosite sequence GAKRH description HISTONE_H4 Histone H4 signature. GAKRH source prosite : PS00047 88) chain A residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 89) chain C residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 90) chain B residue 92-114 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357

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