eF-site ID 1eqz-ABCDEFGHIJ PDB Code 1eqz Chain A, B, C, D, E, F, G, H, I, J 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 I:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCT GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT GGTAGAATCTGCAGGTGGATATTGAT J:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCT GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT GGTAGAATCTGCAGGTGGATATTGAT 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 J residue 255 type sequence A description BINDING SITE FOR RESIDUE K J 452 source : AC4 20) chain J residue 256 type sequence A description BINDING SITE FOR RESIDUE K J 452 source : AC4 21) chain A residue 124 type sequence K description BINDING SITE FOR RESIDUE K J 453 source : AC5 22) chain J residue 216 type sequence G description BINDING SITE FOR RESIDUE K J 453 source : AC5 23) chain J residue 217 type sequence G description BINDING SITE FOR RESIDUE K J 454 source : AC6 24) chain J residue 227 type sequence G description BINDING SITE FOR RESIDUE K J 455 source : AC7 25) chain J residue 228 type sequence A description BINDING SITE FOR RESIDUE K J 456 source : AC8 26) chain J residue 175 type sequence A description BINDING SITE FOR RESIDUE K J 457 source : AC9 27) chain I residue 97 type sequence G description BINDING SITE FOR RESIDUE K I 458 source : BC1 28) chain I residue 98 type sequence G description BINDING SITE FOR RESIDUE K I 458 source : BC1 29) chain J residue 280 type sequence G description BINDING SITE FOR RESIDUE MN J 459 source : BC2 30) chain I residue 134 type sequence G description BINDING SITE FOR RESIDUE MN I 460 source : BC3 31) chain I residue 140 type sequence T description BINDING SITE FOR RESIDUE MN J 462 source : BC5 32) chain J residue 246 type sequence G description BINDING SITE FOR RESIDUE MN J 462 source : BC5 33) chain I residue 121 type sequence G description BINDING SITE FOR RESIDUE MN I 463 source : BC6 34) chain I residue 70 type sequence G description BINDING SITE FOR RESIDUE MN I 464 source : BC7 35) chain I residue 71 type sequence G description BINDING SITE FOR RESIDUE MN I 464 source : BC7 36) chain I residue 39 type sequence G description BINDING SITE FOR RESIDUE MN I 465 source : BC8 37) chain I residue 40 type sequence G description BINDING SITE FOR RESIDUE MN I 465 source : BC8 38) chain I residue 137 type sequence G description BINDING SITE FOR RESIDUE MN I 466 source : BC9 39) chain I residue 138 type sequence G description BINDING SITE FOR RESIDUE MN I 466 source : BC9 40) chain J residue 185 type sequence G description BINDING SITE FOR RESIDUE MN J 467 source : CC1 41) chain J residue 186 type sequence G description BINDING SITE FOR RESIDUE MN J 467 source : CC1 42) chain J residue 267 type sequence G description BINDING SITE FOR RESIDUE MN J 468 source : CC2 43) chain J residue 147 type sequence A description BINDING SITE FOR RESIDUE MN J 469 source : CC3 44) chain I residue 100 type sequence G description BINDING SITE FOR RESIDUE MN I 470 source : CC4 45) chain I residue 1 type sequence A description BINDING SITE FOR RESIDUE MN I 471 source : CC5 46) chain I residue 17 type sequence A description BINDING SITE FOR RESIDUE MN I 472 source : CC6 47) chain I residue 18 type sequence G description BINDING SITE FOR RESIDUE MN I 472 source : CC6 48) chain I residue 124 type sequence A description BINDING SITE FOR RESIDUE MN I 473 source : CC7 49) chain I residue 125 type sequence G description BINDING SITE FOR RESIDUE MN I 473 source : CC7 50) chain D residue 16-20 type DNA_BIND sequence KRHRK description source Swiss-Prot : SWS_FT_FI1 51) chain H residue 16-20 type DNA_BIND sequence KRHRK description source Swiss-Prot : SWS_FT_FI1 52) chain B residue 21 type DNA_BIND sequence T description source Swiss-Prot : SWS_FT_FI1 53) chain F residue 21 type DNA_BIND sequence T description source Swiss-Prot : SWS_FT_FI1 54) chain D residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 55) chain H residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 56) chain E residue 120 type MOD_RES sequence T description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 57) chain D residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 58) chain H residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 59) chain C residue 64 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 60) chain G residue 18 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 61) chain G residue 23 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 62) chain G residue 64 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 63) chain C residue 37 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI15 64) chain G residue 37 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI15 65) chain C residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 66) chain C residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 67) chain G residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 68) chain G residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 69) chain C residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI20 70) chain G residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI20 71) chain C residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 72) chain G residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 73) chain C residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI22 74) chain G residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI22 75) chain C residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI23 76) chain G residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI23 77) 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 78) 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 79) 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 80) 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 81) 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 82) 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 83) chain C residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 84) chain G residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 85) chain C residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI17 86) chain C residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI17 87) chain G residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI17 88) chain G residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI17 89) chain C residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI18 90) chain G residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI18 91) chain G residue 17 type MOD_RES sequence R description Phosphoserine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI2 92) 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 93) 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 94) chain F residue 121 type MOD_RES sequence Y description N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI4 95) chain D residue 16 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 96) chain D residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 97) chain D residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 98) chain H residue 8 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 99) chain H residue 16 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 100) chain H residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 101) chain H residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 102) chain D residue 20 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 103) chain H residue 12 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 104) chain H residue 20 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 105) chain D residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 106) chain D residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 107) chain H residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 108) chain H residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 109) chain D residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 110) chain H residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 111) chain E residue 119 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 112) chain E residue 120 type MOD_RES sequence T description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 113) chain D residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 114) chain D residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 115) chain H residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 116) chain H residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 117) chain D residue 14-18 type prosite sequence GAKRH description HISTONE_H4 Histone H4 signature. GAKRH source prosite : PS00047 118) chain A residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 119) chain C residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 120) chain B residue 92-114 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357

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