eF-site ID 1s32-ABCDEFGHIJ PDB Code 1s32 Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title Molecular Recognition of the Nucleosomal 'Supergroove' Classification STRUCTURAL PROTEIN/DNA Compound palindromic alpha-satellite 146 bp DNA fragment Source Homo sapiens (Human) (A0A8J0U496_XENLA) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA B:  LRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVF LENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFG G C:  AKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYL AAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDE ELNKLLGRVTIAQGGVLPNIQSVLLPK D:  DGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNS FVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPG ELAKHAVSEGTKAVTKYTSAK E:  KPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ DFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKR VTIMPKDIQLARRIRGERA F:  AKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEET RGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQG RTLYGFGG G:  KAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLA AVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEE LNKLLGRVTIAQGGVLPNIQSVLLPKK H:  KRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVN DVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELA KHAVSEGTKAVTKYTSAK 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 2001 source : AC1 2) chain E residue 677 type sequence D description BINDING SITE FOR RESIDUE MN E 2001 source : AC1 3) chain J residue 246 type sequence G description BINDING SITE FOR RESIDUE MN J 2002 source : AC2 4) chain I residue 70 type sequence G description BINDING SITE FOR RESIDUE MN I 2003 source : AC3 5) chain I residue 71 type sequence G description BINDING SITE FOR RESIDUE MN I 2003 source : AC3 6) chain I residue 134 type sequence G description BINDING SITE FOR RESIDUE MN I 2004 source : AC4 7) chain J residue 280 type sequence G description BINDING SITE FOR RESIDUE MN J 2005 source : AC5 8) chain I residue 100 type sequence G description BINDING SITE FOR RESIDUE MN I 2006 source : AC6 9) chain I residue 39 type sequence G description BINDING SITE FOR RESIDUE MN I 2007 source : AC7 10) chain I residue 40 type sequence G description BINDING SITE FOR RESIDUE MN I 2007 source : AC7 11) chain J residue 266 type sequence T description BINDING SITE FOR RESIDUE MN J 2008 source : AC8 12) chain J residue 267 type sequence G description BINDING SITE FOR RESIDUE MN J 2008 source : AC8 13) chain I residue 121 type sequence G description BINDING SITE FOR RESIDUE MN I 2009 source : AC9 14) chain J residue 217 type sequence G description BINDING SITE FOR RESIDUE MN J 2010 source : BC1 15) chain J residue 227 type sequence G description BINDING SITE FOR RESIDUE MN J 2011 source : BC2 16) chain J residue 185 type sequence G description BINDING SITE FOR RESIDUE MN J 2013 source : BC4 17) chain J residue 186 type sequence G description BINDING SITE FOR RESIDUE MN J 2013 source : BC4 18) chain I residue 137 type sequence G description BINDING SITE FOR RESIDUE MN I 2014 source : BC5 19) chain I residue 138 type sequence G description BINDING SITE FOR RESIDUE MN I 2014 source : BC5 20) chain E residue 721 type sequence P description BINDING SITE FOR RESIDUE CL E 2015 source : BC6 21) chain E residue 722 type sequence K description BINDING SITE FOR RESIDUE CL E 2015 source : BC6 22) chain G residue 1044 type sequence G description BINDING SITE FOR RESIDUE CL G 2016 source : BC7 23) chain G residue 1045 type sequence A description BINDING SITE FOR RESIDUE CL G 2016 source : BC7 24) chain G residue 1046 type sequence G description BINDING SITE FOR RESIDUE CL G 2016 source : BC7 25) chain G residue 1047 type sequence A description BINDING SITE FOR RESIDUE CL G 2016 source : BC7 26) chain H residue 1487 type sequence T description BINDING SITE FOR RESIDUE CL G 2016 source : BC7 27) chain H residue 1488 type sequence S description BINDING SITE FOR RESIDUE CL G 2016 source : BC7 28) chain A residue 521 type sequence P description BINDING SITE FOR RESIDUE CL A 2017 source : BC8 29) chain A residue 522 type sequence K description BINDING SITE FOR RESIDUE CL A 2017 source : BC8 30) chain C residue 846 type sequence G description BINDING SITE FOR RESIDUE CL D 2018 source : BC9 31) chain C residue 847 type sequence A description BINDING SITE FOR RESIDUE CL D 2018 source : BC9 32) chain D residue 1287 type sequence T description BINDING SITE FOR RESIDUE CL D 2018 source : BC9 33) chain D residue 1288 type sequence S description BINDING SITE FOR RESIDUE CL D 2018 source : BC9 34) chain I residue 31 type sequence G description BINDING SITE FOR RESIDUE IMT I 1601 source : CC1 35) chain I residue 32 type sequence T description BINDING SITE FOR RESIDUE IMT I 1601 source : CC1 36) chain I residue 32 type sequence T description BINDING SITE FOR RESIDUE PYB I 1602 source : CC2 37) chain I residue 33 type sequence G description BINDING SITE FOR RESIDUE PYB I 1602 source : CC2 38) chain I residue 33 type sequence G description BINDING SITE FOR RESIDUE IMT I 1603 source : CC3 39) chain I residue 34 type sequence T description BINDING SITE FOR RESIDUE IMT I 1603 source : CC3 40) chain I residue 35 type sequence A description BINDING SITE FOR RESIDUE IMT I 1603 source : CC3 41) chain I residue 34 type sequence T description BINDING SITE FOR RESIDUE PYB I 1604 source : CC4 42) chain I residue 35 type sequence A description BINDING SITE FOR RESIDUE PYB I 1604 source : CC4 43) chain I residue 36 type sequence T description BINDING SITE FOR RESIDUE PYB I 1604 source : CC4 44) chain J residue 259 type sequence A description BINDING SITE FOR RESIDUE ABU I 1605 source : CC5 45) chain J residue 260 type sequence C description BINDING SITE FOR RESIDUE ABU I 1605 source : CC5 46) chain J residue 259 type sequence A description BINDING SITE FOR RESIDUE PYB I 1606 source : CC6 47) chain J residue 260 type sequence C description BINDING SITE FOR RESIDUE PYB I 1606 source : CC6 48) chain J residue 261 type sequence A description BINDING SITE FOR RESIDUE PYB I 1606 source : CC6 49) chain J residue 260 type sequence C description BINDING SITE FOR RESIDUE PYB I 1607 source : CC7 50) chain J residue 261 type sequence A description BINDING SITE FOR RESIDUE PYB I 1607 source : CC7 51) chain J residue 261 type sequence A description BINDING SITE FOR RESIDUE PYB I 1608 source : CC8 52) chain J residue 262 type sequence C description BINDING SITE FOR RESIDUE PYB I 1608 source : CC8 53) chain J residue 263 type sequence T description BINDING SITE FOR RESIDUE PYB I 1608 source : CC8 54) chain I residue 31 type sequence G description BINDING SITE FOR RESIDUE PYB I 1609 source : CC9 55) chain J residue 262 type sequence C description BINDING SITE FOR RESIDUE PYB I 1609 source : CC9 56) chain J residue 263 type sequence T description BINDING SITE FOR RESIDUE PYB I 1609 source : CC9 57) chain I residue 30 type sequence A description BINDING SITE FOR RESIDUE BAL I 1610 source : DC1 58) chain I residue 31 type sequence G description BINDING SITE FOR RESIDUE BAL I 1610 source : DC1 59) chain J residue 263 type sequence T description BINDING SITE FOR RESIDUE BAL I 1610 source : DC1 60) chain I residue 29 type sequence A description BINDING SITE FOR RESIDUE DIB I 1611 source : DC2 61) chain I residue 30 type sequence A description BINDING SITE FOR RESIDUE DIB I 1611 source : DC2 62) chain J residue 265 type sequence T description BINDING SITE FOR RESIDUE DIB I 1611 source : DC2 63) chain J residue 266 type sequence T description BINDING SITE FOR RESIDUE DIB I 1611 source : DC2 64) chain J residue 178 type sequence T description BINDING SITE FOR RESIDUE IMT I 1621 source : DC3 65) chain J residue 178 type sequence T description BINDING SITE FOR RESIDUE PYB I 1622 source : DC4 66) chain J residue 179 type sequence G description BINDING SITE FOR RESIDUE PYB I 1622 source : DC4 67) chain J residue 179 type sequence G description BINDING SITE FOR RESIDUE IMT I 1623 source : DC5 68) chain J residue 180 type sequence T description BINDING SITE FOR RESIDUE IMT I 1623 source : DC5 69) chain J residue 181 type sequence A description BINDING SITE FOR RESIDUE IMT I 1623 source : DC5 70) chain I residue 113 type sequence A description BINDING SITE FOR RESIDUE PYB I 1624 source : DC6 71) chain J residue 180 type sequence T description BINDING SITE FOR RESIDUE PYB I 1624 source : DC6 72) chain J residue 181 type sequence A description BINDING SITE FOR RESIDUE PYB I 1624 source : DC6 73) chain J residue 182 type sequence T description BINDING SITE FOR RESIDUE PYB I 1624 source : DC6 74) chain I residue 113 type sequence A description BINDING SITE FOR RESIDUE ABU I 1625 source : DC7 75) chain J residue 181 type sequence A description BINDING SITE FOR RESIDUE ABU I 1625 source : DC7 76) chain I residue 113 type sequence A description BINDING SITE FOR RESIDUE PYB I 1626 source : DC8 77) chain I residue 114 type sequence C description BINDING SITE FOR RESIDUE PYB I 1626 source : DC8 78) chain I residue 115 type sequence A description BINDING SITE FOR RESIDUE PYB I 1626 source : DC8 79) chain I residue 114 type sequence C description BINDING SITE FOR RESIDUE PYB I 1627 source : DC9 80) chain I residue 115 type sequence A description BINDING SITE FOR RESIDUE PYB I 1627 source : DC9 81) chain I residue 116 type sequence C description BINDING SITE FOR RESIDUE PYB I 1627 source : DC9 82) chain I residue 115 type sequence A description BINDING SITE FOR RESIDUE PYB I 1628 source : EC1 83) chain I residue 116 type sequence C description BINDING SITE FOR RESIDUE PYB I 1628 source : EC1 84) chain I residue 117 type sequence T description BINDING SITE FOR RESIDUE PYB I 1628 source : EC1 85) chain G residue 1013 type sequence K description BINDING SITE FOR RESIDUE PYB I 1629 source : EC2 86) chain I residue 116 type sequence C description BINDING SITE FOR RESIDUE PYB I 1629 source : EC2 87) chain I residue 117 type sequence T description BINDING SITE FOR RESIDUE PYB I 1629 source : EC2 88) chain I residue 118 type sequence T description BINDING SITE FOR RESIDUE PYB I 1629 source : EC2 89) chain J residue 177 type sequence G description BINDING SITE FOR RESIDUE PYB I 1629 source : EC2 90) chain G residue 1014 type sequence A description BINDING SITE FOR RESIDUE BAL I 1630 source : EC3 91) chain J residue 176 type sequence A description BINDING SITE FOR RESIDUE BAL I 1630 source : EC3 92) chain J residue 177 type sequence G description BINDING SITE FOR RESIDUE BAL I 1630 source : EC3 93) chain I residue 119 type sequence T description BINDING SITE FOR RESIDUE DIB I 1631 source : EC4 94) chain I residue 120 type sequence T description BINDING SITE FOR RESIDUE DIB I 1631 source : EC4 95) chain J residue 175 type sequence A description BINDING SITE FOR RESIDUE DIB I 1631 source : EC4 96) chain J residue 176 type sequence A description BINDING SITE FOR RESIDUE DIB I 1631 source : EC4 97) chain I residue 113 type sequence A description BINDING SITE FOR RESIDUE OGG J 1700 source : EC5 98) chain J residue 259 type sequence A description BINDING SITE FOR RESIDUE OGG J 1700 source : EC5 99) chain A residue 486 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 100) chain E residue 686 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 101) chain A residue 515 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 102) chain E residue 715 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 103) chain A residue 522 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 104) chain E residue 722 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 105) chain A residue 510 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 106) chain E residue 710 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 107) chain A residue 441 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 108) chain E residue 641 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 109) chain A residue 456 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 110) chain A residue 479 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 111) chain E residue 656 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 112) chain E residue 679 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 113) chain A residue 457 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 114) chain E residue 657 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 115) chain A residue 480 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 116) chain A residue 507 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 117) chain E residue 680 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 118) chain E residue 707 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 119) chain D residue 1309 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 120) chain H residue 1509 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 121) chain G residue 1095 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 122) chain D residue 1317 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 123) chain G residue 1036 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 124) chain H residue 1517 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 125) chain C residue 874 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 126) chain C residue 875 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 127) chain G residue 1074 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 128) chain G residue 1075 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 129) chain F residue 216 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 130) chain F residue 244 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 131) chain F residue 279 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 132) chain C residue 904 type MOD_RES sequence Q description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 133) chain G residue 1104 type MOD_RES sequence Q description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 134) chain F residue 220 type MOD_RES sequence K description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 135) chain C residue 918 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 136) chain G residue 1118 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 137) chain F residue 231 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 138) chain F residue 291 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 139) chain C residue 813 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 140) chain F residue 247 type CROSSLNK sequence S description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 141) chain C residue 815 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 142) chain G residue 1013 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 143) chain G residue 1015 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 144) chain G residue 1119 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 145) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 146) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 147) chain F residue 251 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 148) chain F residue 288 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 149) chain A residue 466-474 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 150) chain D residue 1289-1311 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 151) chain C residue 821-827 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 152) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 153) chain E residue 664 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 154) chain F residue 259 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 155) chain A residue 464 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 156) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 157) chain F residue 277 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 158) 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 159) 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 160) 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 161) 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

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