eF-site ID 6jm9-ABCDEFGHIJX PDB Code 6jm9 Chain A, B, C, D, E, F, G, H, I, J, X click to enlarge Title cryo-EM structure of DOT1L bound to unmodified nucleosome Classification GENE REGULATION Compound DNA strand I Source (DOT1L_HUMAN) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA B:  VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF GG C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKKT D:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSAK E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA F:  KRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETR GVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGR TLYGFGG G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKK H:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSAK I:  CACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTC CATCAAAAGGCATGTTCAGCTGAATTCAGCTGAACATGCC TTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATC TGC J:  GCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCA AAAGGCATGTTCAGCTGAATTCAGCTGAACATGCCTTTTG ATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAG GTG X:  LELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWV CEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDS IHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVTDPEK LNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGS GVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRK WMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFA FGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNL SDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILEN YFSSLKNP Description Functional site 1) chain X residue 133 type sequence P description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 2) chain X residue 135 type sequence V description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 3) chain X residue 136 type sequence Y description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 4) chain X residue 138 type sequence E description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 5) chain X residue 139 type sequence T description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 6) chain X residue 161 type sequence D description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 7) chain X residue 163 type sequence G description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 8) chain X residue 164 type sequence S description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 9) chain X residue 186 type sequence E description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 10) chain X residue 187 type sequence K description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 11) chain X residue 188 type sequence A description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 12) chain X residue 222 type sequence D description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 13) chain X residue 223 type sequence F description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 14) chain X residue 224 type sequence L description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 15) chain X residue 225 type sequence S description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 16) chain X residue 239 type sequence F description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 17) chain X residue 241 type sequence N description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 18) chain X residue 245 type sequence F description binding site for Di-peptide SAM X 500 and GLY X 137 source : AC1 19) chain X residue 133 type sequence P description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 20) chain X residue 135 type sequence V description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 21) chain X residue 136 type sequence Y description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 22) chain X residue 137 type sequence G description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 23) chain X residue 138 type sequence E description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 24) chain X residue 139 type sequence T description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 25) chain X residue 161 type sequence D description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 26) chain X residue 163 type sequence G description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 27) chain X residue 164 type sequence S description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 28) chain X residue 185 type sequence V description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 29) chain X residue 186 type sequence E description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 30) chain X residue 187 type sequence K description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 31) chain X residue 188 type sequence A description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 32) chain X residue 222 type sequence D description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 33) chain X residue 224 type sequence L description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 34) chain X residue 225 type sequence S description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 35) chain X residue 239 type sequence F description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 36) chain X residue 241 type sequence N description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 37) chain X residue 245 type sequence F description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC2 38) chain X residue 133 type sequence P description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 39) chain X residue 135 type sequence V description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 40) chain X residue 136 type sequence Y description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 41) chain X residue 137 type sequence G description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 42) chain X residue 138 type sequence E description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 43) chain X residue 139 type sequence T description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 44) chain X residue 161 type sequence D description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 45) chain X residue 163 type sequence G description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 46) chain X residue 164 type sequence S description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 47) chain X residue 185 type sequence V description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 48) chain X residue 186 type sequence E description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 49) chain X residue 187 type sequence K description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 50) chain X residue 188 type sequence A description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 51) chain X residue 222 type sequence D description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 52) chain X residue 224 type sequence L description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 53) chain X residue 225 type sequence S description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 54) chain X residue 239 type sequence F description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 55) chain X residue 241 type sequence N description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 56) chain X residue 245 type sequence F description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC3 57) chain X residue 133 type sequence P description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 58) chain X residue 135 type sequence V description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 59) chain X residue 136 type sequence Y description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 60) chain X residue 137 type sequence G description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 61) chain X residue 138 type sequence E description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 62) chain X residue 139 type sequence T description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 63) chain X residue 161 type sequence D description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 64) chain X residue 163 type sequence G description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 65) chain X residue 164 type sequence S description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 66) chain X residue 185 type sequence V description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 67) chain X residue 186 type sequence E description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 68) chain X residue 187 type sequence K description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 69) chain X residue 188 type sequence A description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 70) chain X residue 222 type sequence D description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 71) chain X residue 224 type sequence L description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 72) chain X residue 225 type sequence S description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 73) chain X residue 239 type sequence F description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 74) chain X residue 241 type sequence N description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 75) chain X residue 245 type sequence F description binding site for Di-peptide SAM X 500 and PHE X 223 source : AC4 76) chain X residue 133 type sequence P description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 77) chain X residue 135 type sequence V description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 78) chain X residue 136 type sequence Y description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 79) chain X residue 137 type sequence G description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 80) chain X residue 138 type sequence E description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 81) chain X residue 139 type sequence T description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 82) chain X residue 161 type sequence D description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 83) chain X residue 163 type sequence G description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 84) chain X residue 164 type sequence S description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 85) chain X residue 186 type sequence E description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 86) chain X residue 187 type sequence K description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 87) chain X residue 188 type sequence A description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 88) chain X residue 222 type sequence D description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 89) chain X residue 223 type sequence F description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 90) chain X residue 225 type sequence S description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 91) chain X residue 239 type sequence F description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 92) chain X residue 241 type sequence N description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 93) chain X residue 245 type sequence F description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 94) chain X residue 253 type sequence L description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 95) chain X residue 256 type sequence R description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC5 96) chain X residue 133 type sequence P description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 97) chain X residue 135 type sequence V description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 98) chain X residue 136 type sequence Y description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 99) chain X residue 137 type sequence G description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 100) chain X residue 138 type sequence E description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 101) chain X residue 139 type sequence T description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 102) chain X residue 161 type sequence D description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 103) chain X residue 163 type sequence G description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 104) chain X residue 164 type sequence S description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 105) chain X residue 186 type sequence E description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 106) chain X residue 187 type sequence K description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 107) chain X residue 188 type sequence A description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 108) chain X residue 222 type sequence D description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 109) chain X residue 223 type sequence F description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 110) chain X residue 225 type sequence S description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 111) chain X residue 239 type sequence F description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 112) chain X residue 241 type sequence N description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 113) chain X residue 245 type sequence F description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 114) chain X residue 253 type sequence L description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 115) chain X residue 256 type sequence R description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC6 116) chain X residue 133 type sequence P description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 117) chain X residue 135 type sequence V description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 118) chain X residue 136 type sequence Y description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 119) chain X residue 137 type sequence G description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 120) chain X residue 138 type sequence E description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 121) chain X residue 139 type sequence T description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 122) chain X residue 161 type sequence D description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 123) chain X residue 163 type sequence G description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 124) chain X residue 164 type sequence S description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 125) chain X residue 186 type sequence E description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 126) chain X residue 187 type sequence K description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 127) chain X residue 188 type sequence A description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 128) chain X residue 222 type sequence D description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 129) chain X residue 223 type sequence F description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 130) chain X residue 225 type sequence S description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 131) chain X residue 239 type sequence F description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 132) chain X residue 241 type sequence N description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 133) chain X residue 245 type sequence F description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 134) chain X residue 253 type sequence L description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 135) chain X residue 256 type sequence R description binding site for Di-peptide SAM X 500 and LEU X 224 source : AC7 136) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 137) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 138) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 139) chain X residue 186 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI1 140) chain X residue 222 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 141) chain X residue 136 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI1 142) chain X residue 159 type BINDING sequence F description source Swiss-Prot : SWS_FT_FI1 143) chain X residue 297 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 144) chain B residue 44 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 145) chain H residue 117 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 146) chain F residue 16 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 147) chain F residue 44 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 148) chain F residue 79 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 149) chain F residue 20 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI3 150) chain B residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI4 151) chain B residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI4 152) chain F residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI4 153) chain F residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI4 154) chain B residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 155) chain F residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 156) chain E residue 80 type MOD_RES sequence T description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 157) chain E residue 107 type MOD_RES sequence T description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 158) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 159) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 160) chain F residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 161) chain F residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 162) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 163) chain F residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 164) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 165) chain F residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 166) 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_FI9 167) 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_FI9 168) 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_FI10 169) 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_FI10

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