eF-site ID 1m1a-ABCDEFGHIJ PDB Code 1m1a Chain A, B, C, D, E, F, G, H, I, J Title LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA Classification STRUCTURAL PROTEIN/DNA Compound Palindromic 146 Base Pair DNA Fragment Source Xenopus laevis (African clawed frog) (A0A8J0U496_XENLA) Sequence A:  KPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ DFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKR VTIMPKDIQLARRIRGERA B:  RDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFL ENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPK D:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSA E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA F:  LGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGL IYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYA LKRQGRTLYGFGG G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKK H:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSA I:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCT GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT GGTAGAATCTGCAGGTGGATATTGAT J:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCT GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT GGTAGAATCTGCAGGTGGATATTGAT Description Functional site 1) chain D residue 1245 type sequence V description BINDING SITE FOR RESIDUE MN E 301 source : AC1 2) chain E residue 677 type sequence D description BINDING SITE FOR RESIDUE MN E 301 source : AC1 3) chain J residue 280 type sequence G description BINDING SITE FOR RESIDUE MN J 302 source : AC2 4) chain J residue 281 type sequence G description BINDING SITE FOR RESIDUE MN J 302 source : AC2 5) chain I residue 134 type sequence G description BINDING SITE FOR RESIDUE MN I 303 source : AC3 6) chain J residue 216 type sequence G description BINDING SITE FOR RESIDUE MN J 304 source : AC4 7) chain I residue 71 type sequence G description BINDING SITE FOR RESIDUE MN I 305 source : AC5 8) chain J residue 267 type sequence G description BINDING SITE FOR RESIDUE MN J 306 source : AC6 9) chain J residue 245 type sequence A description BINDING SITE FOR RESIDUE MN J 308 source : AC7 10) chain J residue 246 type sequence G description BINDING SITE FOR RESIDUE MN J 308 source : AC7 11) chain I residue 121 type sequence G description BINDING SITE FOR RESIDUE MN I 309 source : AC8 12) chain I residue 39 type sequence G description BINDING SITE FOR RESIDUE MN I 310 source : AC9 13) chain I residue 40 type sequence G description BINDING SITE FOR RESIDUE MN I 310 source : AC9 14) chain J residue 283 type sequence G description BINDING SITE FOR RESIDUE IMT J 1901 source : BC1 15) chain J residue 284 type sequence G description BINDING SITE FOR RESIDUE IMT J 1901 source : BC1 16) chain J residue 285 type sequence A description BINDING SITE FOR RESIDUE IMT J 1901 source : BC1 17) chain J residue 284 type sequence G description BINDING SITE FOR RESIDUE IMT J 1902 source : BC2 18) chain J residue 285 type sequence A description BINDING SITE FOR RESIDUE IMT J 1902 source : BC2 19) chain J residue 286 type sequence T description BINDING SITE FOR RESIDUE IMT J 1902 source : BC2 20) chain J residue 285 type sequence A description BINDING SITE FOR RESIDUE PYB J 1903 source : BC3 21) chain J residue 286 type sequence T description BINDING SITE FOR RESIDUE PYB J 1903 source : BC3 22) chain J residue 286 type sequence T description BINDING SITE FOR RESIDUE PYB J 1904 source : BC4 23) chain J residue 287 type sequence A description BINDING SITE FOR RESIDUE PYB J 1904 source : BC4 24) chain J residue 288 type sequence T description BINDING SITE FOR RESIDUE PYB J 1904 source : BC4 25) chain I residue 7 type sequence A description BINDING SITE FOR RESIDUE ABU J 1905 source : BC5 26) chain J residue 287 type sequence A description BINDING SITE FOR RESIDUE ABU J 1905 source : BC5 27) chain J residue 288 type sequence T description BINDING SITE FOR RESIDUE ABU J 1905 source : BC5 28) chain I residue 7 type sequence A description BINDING SITE FOR RESIDUE PYB J 1906 source : BC6 29) chain I residue 8 type sequence T description BINDING SITE FOR RESIDUE PYB J 1906 source : BC6 30) chain I residue 9 type sequence C description BINDING SITE FOR RESIDUE PYB J 1906 source : BC6 31) chain I residue 8 type sequence T description BINDING SITE FOR RESIDUE PYB J 1907 source : BC7 32) chain I residue 9 type sequence C description BINDING SITE FOR RESIDUE PYB J 1907 source : BC7 33) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE PYB J 1907 source : BC7 34) chain I residue 9 type sequence C description BINDING SITE FOR RESIDUE PYB J 1908 source : BC8 35) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE PYB J 1908 source : BC8 36) chain I residue 11 type sequence A description BINDING SITE FOR RESIDUE PYB J 1908 source : BC8 37) chain J residue 284 type sequence G description BINDING SITE FOR RESIDUE PYB J 1908 source : BC8 38) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE PYB J 1909 source : BC9 39) chain I residue 11 type sequence A description BINDING SITE FOR RESIDUE PYB J 1909 source : BC9 40) chain I residue 12 type sequence C description BINDING SITE FOR RESIDUE PYB J 1909 source : BC9 41) chain J residue 283 type sequence G description BINDING SITE FOR RESIDUE PYB J 1909 source : BC9 42) chain I residue 11 type sequence A description BINDING SITE FOR RESIDUE BAL J 1910 source : CC1 43) chain J residue 282 type sequence T description BINDING SITE FOR RESIDUE BAL J 1910 source : CC1 44) chain J residue 283 type sequence G description BINDING SITE FOR RESIDUE BAL J 1910 source : CC1 45) chain J residue 282 type sequence T description BINDING SITE FOR RESIDUE DIB J 1911 source : CC2 46) chain A residue 456 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 47) 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 48) chain E residue 656 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 49) chain F residue 291 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 B residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 51) chain F residue 247 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 52) chain C residue 815 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 53) chain G residue 1015 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 54) chain G residue 1119 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 55) chain A residue 515 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI16 56) chain E residue 715 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI16 57) chain A residue 522 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI17 58) chain E residue 722 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI17 59) chain A residue 457 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI14 60) chain E residue 657 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI14 61) chain A residue 480 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI15 62) chain E residue 680 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI15 63) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 64) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 65) chain F residue 251 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 66) chain F residue 288 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 67) chain A residue 466-474 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 68) chain C residue 821-827 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 69) chain D residue 1289-1311 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 70) chain B residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 71) chain B residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 72) chain F residue 216 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 73) chain F residue 244 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 74) chain F residue 279 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 75) chain F residue 212 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 76) chain F residue 220 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 77) chain B residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 78) chain B residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 79) chain F residue 231 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 80) chain F residue 291 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 81) chain F residue 216-220 type DNA_BIND sequence KRHRK description source Swiss-Prot : SWS_FT_FI1 82) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 83) chain F residue 259 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 84) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 85) chain F residue 277 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 86) 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 87) chain F residue 231 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 88) chain G residue 1095 type MOD_RES sequence K description Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI3 89) chain H residue 1517 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI4

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