eF-site ID 2jj2-ABCDEFGHIJKLMN PDB Code 2jj2 Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N Title The Structure of F1-ATPase inhibited by quercetin. Classification HYDROLASE Compound ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM Source ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS; Sequence A:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM KQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITK FENAFLSHVISQHQALLSKIRTDGKISEESDAKLKEIVTN FLAGFEA B:  VDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGM SLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEE LLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISV REPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDT IINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTD ADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGK HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLH SRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNV ISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRA MKQVAGTMKLELAQYREVALDAATQQLLSRGVRLTELLKQ GQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLS HVISQHQALLSKIRTDGKISEESDAKLKEIVTNFLAGFE C:  ILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEF SSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIV DVPVGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPG IIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGK TSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQ LVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGE YFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYP GDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVS AYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVG SAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQ QLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDK LEPSKITKFENAFLSHVISQHQALLSKIRTDGKISEESDA KLKEIVTNFLAGFEA D:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLAE E:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA F:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA G:  ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKP ARVYGVGSSDRGLCGAIHSSVAKQMIGVGDKIRSIKEVGR RPPTFGDIFNRFRSVISYKTEYSLANIIYYSLKESTTSEQ SARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEI ISGAAAL H:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM KQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITK FENAFLSHVISQHQALLSKIRTDGKISEESDAKLKEIVTN FLAGFEA I:  VDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGM SLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEE LLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISV REPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDT IINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTD ADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGK HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLH SRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNV ISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRA MKQVAGTMKLELAQYREVALDAATQQLLSRGVRLTELLKQ GQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLS HVISQHQALLSKIRTDGKISEESDAKLKEIVTNFLAGFE J:  ILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEF SSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIV DVPVGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPG IIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGK TSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQ LVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGE YFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYP GDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVS AYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVG SAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQ QLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDK LEPSKITKFENAFLSHVISQHQALLSKIRTDGKISEESDA KLKEIVTNFLAGFEA K:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLAE L:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA M:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA N:  ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKP ARVYGVGSSDRGLCGAIHSSVAKQMIGVGDKIRSIKEVGR RPPTFGDIFNRFRSVISYKTEYSLANIIYYSLKESTTSEQ SARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEI ISGAAAL Description Functional site 1) chain A residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 2) chain A residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 3) chain A residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 4) chain A residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 5) chain A residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 6) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 7) chain A residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 8) chain A residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 9) chain A residue 363 type sequence P description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 10) chain A residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 11) chain A residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP A 1511 source : AC1 12) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE MG A 1512 source : AC2 13) chain A residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL A 1513 source : AC3 14) chain A residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1513 source : AC3 15) chain A residue 245 type sequence L description BINDING SITE FOR RESIDUE GOL A 1513 source : AC3 16) chain A residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1513 source : AC3 17) chain A residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL A 1513 source : AC3 18) chain A residue 291 type sequence R description BINDING SITE FOR RESIDUE GOL A 1514 source : AC4 19) chain A residue 294 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1514 source : AC4 20) chain A residue 295 type sequence P description BINDING SITE FOR RESIDUE GOL A 1514 source : AC4 21) chain A residue 296 type sequence G description BINDING SITE FOR RESIDUE GOL A 1514 source : AC4 22) chain A residue 337 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1514 source : AC4 23) chain E residue 266 type sequence S description BINDING SITE FOR RESIDUE GOL A 1514 source : AC4 24) chain E residue 280 type sequence G description BINDING SITE FOR RESIDUE GOL A 1514 source : AC4 25) chain B residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 26) chain B residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 27) chain B residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 28) chain B residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 29) chain B residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 30) chain B residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 31) chain B residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 32) chain B residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 33) chain B residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 34) chain B residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 35) chain B residue 431 type sequence G description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 36) chain B residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 37) chain E residue 356 type sequence R description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 38) chain E residue 359 type sequence D description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 39) chain B residue 176 type sequence T description BINDING SITE FOR RESIDUE MG B 1511 source : AC6 40) chain B residue 129 type sequence V description BINDING SITE FOR RESIDUE GOL B 1512 source : AC7 41) chain B residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL B 1512 source : AC7 42) chain B residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1512 source : AC7 43) chain B residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1512 source : AC7 44) chain B residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL B 1512 source : AC7 45) chain B residue 290 type sequence G description BINDING SITE FOR RESIDUE GOL B 1513 source : AC8 46) chain B residue 291 type sequence R description BINDING SITE FOR RESIDUE GOL B 1513 source : AC8 47) chain B residue 294 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1513 source : AC8 48) chain B residue 337 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1513 source : AC8 49) chain F residue 266 type sequence S description BINDING SITE FOR RESIDUE GOL B 1513 source : AC8 50) chain F residue 279 type sequence V description BINDING SITE FOR RESIDUE GOL B 1513 source : AC8 51) chain C residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 52) chain C residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 53) chain C residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 54) chain C residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 55) chain C residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 56) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 57) chain C residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 58) chain C residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 59) chain C residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 60) chain C residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 61) chain C residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 62) chain F residue 368 type sequence Y description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 63) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE MG C 1512 source : BC1 64) chain C residue 62 type sequence M description BINDING SITE FOR RESIDUE GOL C 1513 source : BC2 65) chain C residue 129 type sequence V description BINDING SITE FOR RESIDUE GOL C 1513 source : BC2 66) chain C residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL C 1513 source : BC2 67) chain C residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL C 1513 source : BC2 68) chain C residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL C 1513 source : BC2 69) chain C residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL C 1513 source : BC2 70) chain C residue 372 type sequence S description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 71) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 72) chain D residue 157 type sequence G description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 73) chain D residue 159 type sequence G description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 74) chain D residue 160 type sequence V description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 75) chain D residue 161 type sequence G description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 76) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 77) chain D residue 163 type sequence T description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 78) chain D residue 164 type sequence V description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 79) chain D residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 80) chain D residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 81) chain D residue 421 type sequence A description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 82) chain D residue 424 type sequence F description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 83) chain D residue 425 type sequence T description BINDING SITE FOR RESIDUE ADP D 1476 source : BC3 84) chain D residue 163 type sequence T description BINDING SITE FOR RESIDUE MG D 1477 source : BC4 85) chain D residue 256 type sequence D description BINDING SITE FOR RESIDUE MG D 1477 source : BC4 86) chain C residue 344 type sequence S description BINDING SITE FOR RESIDUE AZI D 1478 source : BC5 87) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE AZI D 1478 source : BC5 88) chain D residue 158 type sequence A description BINDING SITE FOR RESIDUE AZI D 1478 source : BC5 89) chain D residue 159 type sequence G description BINDING SITE FOR RESIDUE AZI D 1478 source : BC5 90) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE AZI D 1478 source : BC5 91) chain D residue 311 type sequence Y description BINDING SITE FOR RESIDUE AZI D 1478 source : BC5 92) chain D residue 231 type sequence R description BINDING SITE FOR RESIDUE GOL D 1479 source : BC6 93) chain D residue 265 type sequence G description BINDING SITE FOR RESIDUE GOL D 1479 source : BC6 94) chain D residue 274 type sequence R description BINDING SITE FOR RESIDUE GOL D 1479 source : BC6 95) chain E residue 157 type sequence G description BINDING SITE FOR RESIDUE PO4 E 1475 source : BC7 96) chain E residue 158 type sequence A description BINDING SITE FOR RESIDUE PO4 E 1475 source : BC7 97) chain E residue 159 type sequence G description BINDING SITE FOR RESIDUE PO4 E 1475 source : BC7 98) chain E residue 162 type sequence K description BINDING SITE FOR RESIDUE PO4 E 1475 source : BC7 99) chain E residue 163 type sequence T description BINDING SITE FOR RESIDUE PO4 E 1475 source : BC7 100) chain B residue 343 type sequence I description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 101) chain B residue 344 type sequence S description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 102) chain B residue 371 type sequence V description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 103) chain B residue 373 type sequence R description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 104) chain F residue 158 type sequence A description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 105) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 106) chain F residue 160 type sequence V description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 107) chain F residue 161 type sequence G description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 108) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 109) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 110) chain F residue 164 type sequence V description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 111) chain F residue 189 type sequence R description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 112) chain F residue 345 type sequence Y description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 113) chain F residue 418 type sequence F description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 114) chain F residue 421 type sequence A description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 115) chain F residue 424 type sequence F description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 116) chain F residue 425 type sequence T description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 117) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE MG F 1476 source : BC9 118) chain B residue 291 type sequence R description BINDING SITE FOR RESIDUE QUE G 1273 source : CC1 119) chain B residue 292 type sequence E description BINDING SITE FOR RESIDUE QUE G 1273 source : CC1 120) chain C residue 292 type sequence E description BINDING SITE FOR RESIDUE QUE G 1273 source : CC1 121) chain C residue 293 type sequence A description BINDING SITE FOR RESIDUE QUE G 1273 source : CC1 122) chain F residue 279 type sequence V description BINDING SITE FOR RESIDUE QUE G 1273 source : CC1 123) chain G residue 256 type sequence A description BINDING SITE FOR RESIDUE QUE G 1273 source : CC1 124) chain G residue 259 type sequence T description BINDING SITE FOR RESIDUE QUE G 1273 source : CC1 125) chain G residue 260 type sequence K description BINDING SITE FOR RESIDUE QUE G 1273 source : CC1 126) chain G residue 263 type sequence I description BINDING SITE FOR RESIDUE QUE G 1273 source : CC1 127) chain H residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 128) chain H residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 129) chain H residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 130) chain H residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 131) chain H residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 132) chain H residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 133) chain H residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 134) chain H residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 135) chain H residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 136) chain H residue 363 type sequence P description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 137) chain H residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 138) chain H residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 139) chain H residue 176 type sequence T description BINDING SITE FOR RESIDUE MG H 1512 source : CC3 140) chain H residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL H 1513 source : CC4 141) chain H residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL H 1513 source : CC4 142) chain H residue 245 type sequence L description BINDING SITE FOR RESIDUE GOL H 1513 source : CC4 143) chain H residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL H 1513 source : CC4 144) chain H residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL H 1513 source : CC4 145) chain H residue 290 type sequence G description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 146) chain H residue 291 type sequence R description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 147) chain H residue 294 type sequence Y description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 148) chain H residue 295 type sequence P description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 149) chain H residue 296 type sequence G description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 150) chain H residue 337 type sequence Y description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 151) chain L residue 266 type sequence S description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 152) chain L residue 267 type sequence E description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 153) chain L residue 280 type sequence G description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 154) chain I residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 155) chain I residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 156) chain I residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 157) chain I residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 158) chain I residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 159) chain I residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 160) chain I residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 161) chain I residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 162) chain I residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 163) chain I residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 164) chain I residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 165) chain L residue 356 type sequence R description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 166) chain L residue 359 type sequence D description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 167) chain I residue 176 type sequence T description BINDING SITE FOR RESIDUE MG I 1511 source : CC7 168) chain I residue 129 type sequence V description BINDING SITE FOR RESIDUE GOL I 1512 source : CC8 169) chain I residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL I 1512 source : CC8 170) chain I residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL I 1512 source : CC8 171) chain I residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL I 1512 source : CC8 172) chain I residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL I 1512 source : CC8 173) chain J residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 174) chain J residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 175) chain J residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 176) chain J residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 177) chain J residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 178) chain J residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 179) chain J residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 180) chain J residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 181) chain J residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 182) chain J residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 183) chain J residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 184) chain M residue 368 type sequence Y description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 185) chain J residue 176 type sequence T description BINDING SITE FOR RESIDUE MG J 1512 source : DC1 186) chain J residue 62 type sequence M description BINDING SITE FOR RESIDUE GOL J 1513 source : DC2 187) chain J residue 129 type sequence V description BINDING SITE FOR RESIDUE GOL J 1513 source : DC2 188) chain J residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL J 1513 source : DC2 189) chain J residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL J 1513 source : DC2 190) chain J residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL J 1513 source : DC2 191) chain J residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL J 1513 source : DC2 192) chain J residue 372 type sequence S description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 193) chain J residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 194) chain K residue 159 type sequence G description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 195) chain K residue 160 type sequence V description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 196) chain K residue 161 type sequence G description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 197) chain K residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 198) chain K residue 163 type sequence T description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 199) chain K residue 164 type sequence V description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 200) chain K residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 201) chain K residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 202) chain K residue 421 type sequence A description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 203) chain K residue 424 type sequence F description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 204) chain K residue 425 type sequence T description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 205) chain K residue 163 type sequence T description BINDING SITE FOR RESIDUE MG K 1477 source : DC4 206) chain J residue 344 type sequence S description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 207) chain J residue 373 type sequence R description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 208) chain K residue 158 type sequence A description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 209) chain K residue 159 type sequence G description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 210) chain K residue 162 type sequence K description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 211) chain K residue 189 type sequence R description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 212) chain K residue 311 type sequence Y description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 213) chain K residue 231 type sequence R description BINDING SITE FOR RESIDUE GOL K 1479 source : DC6 214) chain K residue 265 type sequence G description BINDING SITE FOR RESIDUE GOL K 1479 source : DC6 215) chain K residue 274 type sequence R description BINDING SITE FOR RESIDUE GOL K 1479 source : DC6 216) chain K residue 284 type sequence T description BINDING SITE FOR RESIDUE GOL K 1479 source : DC6 217) chain K residue 288 type sequence D description BINDING SITE FOR RESIDUE GOL K 1479 source : DC6 218) chain H residue 215 type sequence Q description BINDING SITE FOR RESIDUE GOL K 1480 source : DC7 219) chain K residue 127 type sequence S description BINDING SITE FOR RESIDUE GOL K 1480 source : DC7 220) chain K residue 129 type sequence E description BINDING SITE FOR RESIDUE GOL K 1480 source : DC7 221) chain K residue 150 type sequence G description BINDING SITE FOR RESIDUE GOL K 1480 source : DC7 222) chain L residue 157 type sequence G description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 223) chain L residue 158 type sequence A description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 224) chain L residue 159 type sequence G description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 225) chain L residue 160 type sequence V description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 226) chain L residue 161 type sequence G description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 227) chain L residue 162 type sequence K description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 228) chain L residue 163 type sequence T description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 229) chain I residue 343 type sequence I description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 230) chain I residue 344 type sequence S description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 231) chain I residue 371 type sequence V description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 232) chain I residue 373 type sequence R description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 233) chain M residue 158 type sequence A description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 234) chain M residue 159 type sequence G description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 235) chain M residue 160 type sequence V description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 236) chain M residue 161 type sequence G description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 237) chain M residue 162 type sequence K description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 238) chain M residue 163 type sequence T description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 239) chain M residue 164 type sequence V description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 240) chain M residue 188 type sequence E description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 241) chain M residue 189 type sequence R description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 242) chain M residue 345 type sequence Y description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 243) chain M residue 418 type sequence F description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 244) chain M residue 421 type sequence A description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 245) chain M residue 424 type sequence F description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 246) chain M residue 425 type sequence T description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 247) chain M residue 163 type sequence T description BINDING SITE FOR RESIDUE MG M 1476 source : EC1 248) chain I residue 291 type sequence R description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 249) chain I residue 292 type sequence E description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 250) chain J residue 292 type sequence E description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 251) chain M residue 278 type sequence A description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 252) chain M residue 279 type sequence V description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 253) chain N residue 256 type sequence A description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 254) chain N residue 259 type sequence T description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 255) chain N residue 260 type sequence K description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 256) chain N residue 263 type sequence I description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 257) chain A residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 258) chain B residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 259) chain C residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 260) chain H residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 261) chain I residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 262) chain J residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 263) chain A residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 264) chain B residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 265) chain C residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 266) chain H residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 267) chain I residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 268) chain J residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 269) chain N residue 14 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 270) chain H residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 271) chain I residue 170 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 272) chain F residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 273) chain K residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 274) chain L residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 275) chain M residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 276) chain H residue 170 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 277) chain I residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 278) chain J residue 170 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 279) chain J residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 280) chain G residue 14 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 281) chain G residue 245 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 282) chain N residue 24 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 283) chain N residue 245 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 284) chain L residue 189 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 285) chain M residue 189 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 286) chain G residue 24 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 287) chain G residue 30 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 288) chain G residue 172 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 289) chain N residue 30 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 290) chain N residue 172 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 291) chain D residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 292) chain E residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 293) chain E residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 294) chain E residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 295) chain E residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 296) chain E residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 297) chain F residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 298) chain F residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 299) chain F residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 300) chain F residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 301) chain F residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 302) chain K residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 303) chain K residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 304) chain K residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 305) chain K residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 306) chain K residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 307) chain L residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 308) chain L residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 309) chain L residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 310) chain L residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 311) chain L residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 312) chain M residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 313) chain M residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 314) chain M residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 315) chain M residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 316) chain M residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 317) chain G residue 129 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 318) chain N residue 129 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 319) chain F residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 320) chain F residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 321) chain K residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 322) chain K residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 323) chain L residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 324) chain L residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 325) chain M residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 326) chain M residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 327) chain H residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 328) chain H residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 329) chain I residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 330) chain I residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 331) chain J residue 22 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 332) chain J residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 333) chain J residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 334) chain F residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 335) chain K residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 336) chain L residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 337) chain M residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 338) chain E residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 339) chain F residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 340) chain K residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 341) chain L residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 342) chain M residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 343) chain D residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 344) chain B residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 345) chain B residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 346) chain B residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 347) chain B residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 348) chain C residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 349) chain C residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 350) chain C residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 351) chain C residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 352) chain C residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 353) chain H residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 354) chain H residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 355) chain H residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 356) chain H residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 357) chain H residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 358) chain I residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 359) chain I residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 360) chain I residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 361) chain I residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 362) chain I residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 363) chain J residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 364) chain J residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 365) chain J residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 366) chain J residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 367) chain J residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 368) chain D residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 369) chain E residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 370) chain F residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 371) chain K residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 372) chain L residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 373) chain M residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 374) chain D residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 375) chain D residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 376) chain E residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 377) chain E residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 378) chain F residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 379) chain F residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 380) chain K residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 381) chain K residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 382) chain L residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 383) chain L residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 384) chain M residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 385) chain M residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 386) chain A residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 387) chain A residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 388) chain A residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 389) chain A residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 390) chain A residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 391) chain B residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 392) chain B residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 393) chain B residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 394) chain B residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 395) chain B residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 396) chain B residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 397) chain B residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 398) chain B residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 399) chain B residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 400) chain B residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 401) chain B residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 402) chain C residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 403) chain C residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 404) chain C residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 405) chain C residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 406) chain C residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 407) chain C residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 408) chain C residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 409) chain C residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 410) chain C residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 411) chain C residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 412) chain C residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 413) chain H residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 414) chain H residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 415) chain H residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 416) chain H residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 417) chain H residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 418) chain H residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 419) chain H residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 420) chain H residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 421) chain H residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 422) chain H residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 423) chain H residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 424) chain I residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 425) chain I residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 426) chain I residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 427) chain I residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 428) chain I residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 429) chain I residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 430) chain I residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 431) chain I residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 432) chain I residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 433) chain I residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 434) chain I residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 435) chain J residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 436) chain J residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 437) chain J residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 438) chain J residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 439) chain J residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 440) chain J residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 441) chain J residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 442) chain J residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 443) chain J residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 444) chain J residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 445) chain J residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 446) chain D residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 447) chain E residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 448) chain F residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 449) chain K residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 450) chain L residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 451) chain M residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 452) chain A residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 453) chain B residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 454) chain C residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 455) chain H residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 456) chain I residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 457) chain J residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 458) chain G residue 258-271 type prosite sequence ITKELIEIISGAAA description ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA source prosite : PS00153 459) chain D residue 162 type catalytic sequence K description 178 source MCSA : MCSA1 460) chain D residue 188 type catalytic sequence E description 178 source MCSA : MCSA1 461) chain D residue 189 type catalytic sequence R description 178 source MCSA : MCSA1 462) chain E residue 162 type catalytic sequence K description 178 source MCSA : MCSA2 463) chain E residue 188 type catalytic sequence E description 178 source MCSA : MCSA2 464) chain E residue 189 type catalytic sequence R description 178 source MCSA : MCSA2 465) chain F residue 162 type catalytic sequence K description 178 source MCSA : MCSA3 466) chain F residue 188 type catalytic sequence E description 178 source MCSA : MCSA3 467) chain F residue 189 type catalytic sequence R description 178 source MCSA : MCSA3 468) chain K residue 162 type catalytic sequence K description 178 source MCSA : MCSA4 469) chain K residue 188 type catalytic sequence E description 178 source MCSA : MCSA4 470) chain K residue 189 type catalytic sequence R description 178 source MCSA : MCSA4 471) chain L residue 162 type catalytic sequence K description 178 source MCSA : MCSA5 472) chain L residue 188 type catalytic sequence E description 178 source MCSA : MCSA5 473) chain L residue 189 type catalytic sequence R description 178 source MCSA : MCSA5 474) chain M residue 162 type catalytic sequence K description 178 source MCSA : MCSA6 475) chain M residue 188 type catalytic sequence E description 178 source MCSA : MCSA6 476) chain M residue 189 type catalytic sequence R description 178 source MCSA : MCSA6 477) chain A residue 363-372 type prosite sequence PAINVGLSVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152 478) chain D residue 346-355 type prosite sequence PAVDPLDSTS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152

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