>Pf6N2E2_240 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_240
MINRLDTQDSGRISVNGVATDELDVVTLRRGIGFMMQSSALFPHQTVAENIGAVPRLLGWSKHKIRQRVSELISLVGLQPEFLDRYPNQLSGGQQSRVALARALASDPPVVLMDEPFAALDPVIRERLQDELVALQRRLHKTIILVTHDMEEAIKIGDRIAIFEGEGKLAQFDTPHNILAHPASEFVKNFIGKDPLLKRLSLMKVSDLPVDEVNCEFKLLLDDKSNPLKWVSESDLPVPELTTVSNNDSLHHALVKILTAPLGVVVRVDEAGGYEGCLSIASFHSALNERRFGSAQ
>SwissProt__Q8ZPK4 Osmoprotectant import ATP-binding protein OsmV; EC 7.6.2.- (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
MIKLENLTKQFVQKKGQPLKAVDNVNLNVPEGEMCVLLGPSGCGKTTTLKMINRLIAPSSGNILINGENTNDMDAVTLRRNIGYVIQQIGLFPNMTIEENITVVPRMLGWDKARCKQRAEELMDMVALDARKFLHRYPKEMSGGQQQRIGVIRALAADPPVLLMDEPFGAVDPINREVIQNQFLDMQRKLKKTVMLVSHDIDEALKLGDRIAVFRQGRIVQCASPDELLAKPANEFVGSFVGQDRTLKRLLLVSAGDVTDQQPTITARPSTPLSEAFGIMDDHDIRAITVIDNDGKPLGFVKRREARNASGICADITHPFRITGKAEDNLRIVLSRLYESNTSWMPIVDEDGRYNGEISQDYIADYLSSGRTRRALNIHENS
>TCDB__Q8Q041 Glycine betaine transporter, ATP-binding protein, component of The glycine betaine uptake porter, GbpABCD (Methanosarcina mazei)
MSFTKLFDRIDSVRLENITKKYGEHFAVKNLNLEIKGGELLILIGRSGSGKTTAIRTINRLIEPDSGAVFINGIDTREFDPVRLRRNIGYVIQNIGLLPHLRISENIGLLLKLEGWKEERIRKRVSELLSLVSLPPESFMDRYPHELSGGQQQRVGLARAMAMDPPLFLMDEPFGALDPLLRTQLQDEFFRIKKELGRTIVFVTHDINEAFRLGDRIAIMNNTELVQVGTPEELIFSPASDLVAEIADSKRKYRHIDALKAGDMMQPINRELTLDPEMPAETALDLIVRNGLELAFVTSPEISGRIGLNDVLKARSEGRELKEAIKPLPLFSSGAPLLEALTELKSRGESMGLVVADNEPVGVLFSDRVLQNLI
>TCDB__Q93A35 BilEA aka OpuBA protein, component of A proline/glycine betaine uptake system. Also reported to be a bile exclusion system that exports oxgall and other bile compounds, BilEA/EB or OpuBA/BB (required for normal virulence) (Listeria monocytogenes)
MIRFDNVSKKYSDDKTAAVNNVTLDIKDGEFFVFIGPSGCGKTTTLKMINRLIPLTTGTIYINEKRISDYDIHELRWDIGYVLQQIALFPHMTIEENIAIVPELKKWSKEKIHDRITELLDSVGLDPESYRHRKPAELSGGEQQRVGVVRALAADPGIILMDEPFSALDPISRQRLQQDISALQKKIKKTIVFVTHDMQEALALGDRICVMQGGEIVQVATPQEIMKNPENDFVKDFLASGHAFNTPILEANFTVNDLIEADLFYSYQTSDGTLGISSTEPVENLVRRIAEEQSIPVTDEAGNYIGTVSNKHVMQFLARHLESSGELV
>SwissProt__Q4FL37 Trimethylamine N-oxide transport system ATP-binding protein TmoW; TMAO transport system ATP-binding protein TmoW; EC 7.6.2.9 (Pelagibacter ubique (strain HTCC1062))
MSDPVIKCESVYKIFGSNAKKMLHEANGNVDAKTFQDNGCIVGVNNASFEVVKGEMLVVMGLSGSGKSTLLRCISRLTDATSGKIYIDGQDLLTLNNKELIELRRNKMGMVFQSFALLPHKTVVENIAFPLQIKGIKTQDSINKAMEMVKLVGLDGRENYFPRELSGGQQQRVGIARSLAVEPDIWFLDEPFSALDPLIRKEMQDEFLRLQEKLQKTIMFITHDFDEALRLADRIAIMKDGVIEQLDTPANIVLNPATEYVRKFTEEVPRGKVLKIADLMEKPETENLSDFKVSKNEIIENVAEKILTQEKSVAVTDENNKIVGSVHPSKIIHTVFSREKK
>SwissProt__P46920 Glycine betaine transport ATP-binding protein OpuAA; Quaternary-amine-transporting ATPase; EC 7.6.2.9 (Bacillus subtilis (strain 168))
MSVDEKPIKIKVEKVSKIFGKQTKKAVQMLANGKTKKEILKATGSTVGVNQADFEVYDGEIFVIMGLSGSGKSTLVRMLNRLIEPTAGNIYIDGDMITNMSKDQLREVRRKKISMVFQKFALFPHRTILENTEYGLELQGVDKQERQQKALESLKLVGLEGFEHQYPDQLSGGMQQRVGLARALTNDPDILLMDEAFSALDPLIRKDMQDELLDLHDNVGKTIIFITHDLDEALRIGDRIVLMKDGNIVQIGTPEEILMNPSNEYVEKFVEDVDLSKVLTAGHIMKRAETVRIDKGPRVALTLMKNLGISSIYAVDKQKKLLGVIYASDAKKAAESDLSLQDILNTEFTTVPENTYLTEIFDVVSDANIPIAVVDEKQRMKGIVVRGALIGALAGNNEYINAEGTNEQTQDPSAQEVK
>biolip__7aheC Opua inhibited inward facing
VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTSGKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYPKQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGKIMQIGTGEEILTNPANDYVKTFVEDTAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDKKRQFRGVVTSEQAIAARKNNQPLKDVMTTDVGTVSKEMLVRDILPIIYDAPTPLAVVDDNGFLKGVLIRGSVLEALAD
>PDB_7ahh_C Opua inhibited inward-facing, sbd docked
VKIKIEHLTKIFGKRIKTALTMVEKGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTS
GKIFIDNQDVATLNKEDLLQVRRKTMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYP
KQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGK
IMQIGTGEEILTNPANDYVKTFVEDTAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDKKRQFRGVVTSEQAIAA
RKNNQPLKDVMTTDVGTVSKEMLVRDILPIIYDAPTPLAVVDDNGFLKGVLIRGSVLEALAD
>TCDB__Q9RQ06 BusAA, component of Uptake system for glycine-betaine (high affinity) and proline (low affinity) (OpuAA-OpuABC) or BusAA-ABC of Lactococcus lactis). BusAA, the ATPase subunit, has a C-terminal tandem cystathionine β-synthase (CBS) domain which is the cytoplasmic K+ sensor for osmotic stress (osmotic strength)while the BusABC subunit has the membrane and receptor domains fused to each other (Biemans-Oldehinkel et al., 2006; Mahmood et al., 2006; Gul et al. 2012). An N-terminal amphipathic α-helix of OpuA is necessary for high activity but is not critical for biogenesis or the ionic regulation of transport (Lactococcus lactis)
MPVKVKIEHLTKIFGKRIKTALTMVEQGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSGSGKSTLLRLLNRLIEPTSGKIFIDDQDVATLNKEDLLQVRRKSMSMVFQNFGLFPHRTILENTEYGLEVQNVPKEERRKRAEKALDNANLLDFKDQYPKQLSGGMQQRVGLARALANDPEILLMDEAFSALDPLIRREMQDELLELQAKFQKTIIFVSHDLNEALRIGDRIAIMKDGKIMQIGTGEEILTNPANDYVKTFVEDVDRAKVITAENIMIPALTTNIDVDGPSVALKKMKTEEVSSLMAVDRKRQFRGVVTSEQAIAARKNNQSLKDVMTTDVGTVTKEMLVRDILPIIYDAPTPLAVVDDQGYLKGILIRGIVLEALADIPDEVEEIEKEEEKND
>reanno__pseudo3_N2E3_AO353_07790 ABC transporter for Carnitine, ATPase component (Pseudomonas fluorescens FW300-N2E3)
MSIIRFDNVDVIFSKDPREALKLLDQGMTRDQILKKTGQIVGVEKASLDIEKGEICVLMGLSGSGKSSLLRCINGLNTVSRGKLFVEHEGRQIDIASCTPAELKMMRTKRIAMVFQKFALMPWLTVRENISFGLEMQGRPEKERRQLVDEKLELVGLTQWRNKKPDELSGGMQQRVGLARALAMDADILLMDEPFSALDPLIRQGLQDELLELQRKLHKTIVFVSHDLDEALKLGSRIAIMKDGRIIQYSKPEEIVLNPADDYVRTFVAHTNPLNVLCGRSLMRTLDNCKRINGSVCLDPGGDSWLDLAEGNTIKGARQNGSSLDLQNWVPGQAVEGLGRRPTLVDSNIGMRDALQIRYQTGNKLVLHDNNKVVGILGDSELYHALLGKNLG
>reanno__pseudo5_N2C3_1_AO356_13805 ABC transporter for Carnitine, ATPase component (Pseudomonas fluorescens FW300-N2C3)
MSIIRFEDVDVIFSNRPKAALDLLDKGFSRPEILQQTGLIVGVEKASLSIEKGEICVLMGLSGSGKSSLLRCINGLNTVSRGKLFVEHEGRQIDIASCSPAELKMMRTKRIAMVFQKFALMPWLTVRENISFGLEMQGRPEKERRKLVDEKLELVGLTQWRNKKPDELSGGMQQRVGLARALAMDADILLMDEPFSALDPLIRQGLQDELLELQRKLQKTIVFVSHDLDEALKLGTRIAIMKDGKIIQYSKPEEIVLNPADDYVRTFVAHTNPLNVLCGRSLMRTLDNCKRINGSVCLDPGGDSWLDLAEGNTIKGARQNGAVLDLQNWAPGQSVEELGRRPTLVDSNIGMRDALQIRYQTGNKLVLHDNQKVVGILGDSELYHALLGKNLG
>reanno__pseudo6_N2E2_Pf6N2E2_4681 ABC transporter for Carnitine, ATPase component (Pseudomonas fluorescens FW300-N2E2)
MSIIRFEDVDVIFSNRPKAALDLLDKGLSRPEILQQTGLIVGVEKASLSIEKGEICVLMGLSGSGKSSLLRCINGLNTVSRGKLFVEHEGRQIDIASCSPAELKMMRTKRIAMVFQKFALMPWLTVRENISFGLEMQGRPEKERRKLVDEKLELVGLTQWRNKKPDELSGGMQQRVGLARALAMDADILLMDEPFSALDPLIRQGLQDELLELQRKLQKTIVFVSHDLDEALKLGTRIAIMKDGKIIQYSKPEEIVLNPADDYVRTFVAHTNPLNVLCGRSLMRTLDNCKRINGSVCLDPGGDSWLDLAEGNTIKGARQNGAALDLQNWVPGQAVEDLGRRPTLVDSNIGMRDALQIRYQTGNKLVLHDNQQVVGILGDSELYHALLGKNLG
>BRENDA__A0A077T7Z1 ABC-type quaternary amine transporter (subunit 1/3) (EC 7.6.2.9) (Vibrio anguillarum serotype O1)
MSPVLEVKNLYKVFGETPQQAFPLLEKGLDKDQIFEQTGLTVGVKDVSLSINEGEIFVIMGLSGSGKSTLVRLLNRLIEPTQGSVLLKGKDIAHISEQELRDVRRKNISMVFQNFALMPHMTVLENAAFGLELSGVVAHERNKSAKEALARVGLDAYCESFPDELSGGMKQRVGLARALANDPDILLMDEAFSALDPLIRTEMQDELIRLQNDDKRTIVFISHDLDEAMRIGDRIAIMQDGIVVQTGTPDEILHHPANDYVSSFFRGVNVASVFSAKDIARKKPAAVFKKHDNDGPAAAMQLLMDHDRDYGIVVDRTNKYSGIVSLDSLKQALKQQTSLSAALLPDIVTVDPELSVSELISQVAEVPYAVPVVDQQGNYYGVITKSRLLQTLDRE
>TCDB__A9CI32 ABC transporter, nucleotide binding/ATPase protein (Proline/glycine betaine), component of High affinity (2mμM) choline uptake porter. The choline binding receptor exhibits a venus fly trap mechanism of substrate binding. (ChoX binds acetyl choline and betaine with low affinity (80μM and 470μM, respectively) (Aktas et al., 2011) (most similar to 3.A.1.12.7) (Agrobacterium tumefaciens (strain C58 / ATCC 33970))
MSDAIIFGNVDIVFGDRPDAALALIDKGSTRDEINAQTGLVLGVANASLSVSEGEILVLMGLSGSGKSTLVRAVNGLAPVVRGSVSVKTKSGYVDPYRCPAKALRDLRMHTVSMVFQQFGLLPWRNVADNVGFGLELSGVPEAERKRMVAEQLELVNLSAWADRKVGELSGGMQQRVGLARAFATGAPILLMDEPFSALDPLIRSRLQDELLEFQSRLKKTILFVSHDLDEAFRIGNRIAMMEGGHIIQCGTPQQIVRQPATPYVADFVQNMNPISMLTAADVMKRGVDERSGRLTVAATALPSSPLIDILDALSKHAGAIGVVDNGAIIGTISADEVVAGLTRHRKK
>biolip__2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg)
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVASAS
>PDB_3puy_A Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVF
QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL
SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF
LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIP
SIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVA
>PDB_3pux_A Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVF
QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL
SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF
LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIP
SIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVA
>PDB_3puw_A Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVF
QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL
SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF
LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIP
SIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVA
>PDB_3puv_A Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4
ASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVF
QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL
SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF
LPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIP
SIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGVA
>PDB_1q12_A Crystal structure of the atp-bound e. Coli malk
VQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS
YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN
LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLP
VKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSI
RQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPG
>ecocyc__MALK-MONOMER maltose ABC transporter ATP binding subunit (EC 7.5.2.1) (Escherichia coli K-12 substr. MG1655)
MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGV
>SwissProt__P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
MASVQLRNVTKAWGDVVVSKDINLDIHDGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGETRMNDIPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVMNQRVNQVAEVLQLAHLLERKPKALSGGQRQRVAIGRTLVAEPRVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIEQVQVELPNRQQIWLPVESRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGHETQIHIQIPAIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGSACRRLHQEPGV
>metacyc__G185E-5409-MONOMER ABC-type trehalose transporter ATP-binding protein (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
MAEIVLDHVNKSYPDGHTAVRDLNLTIADGEFLILVGPSGCGKTTTLNMIAGLEDISSGELRIAGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKMRKADIAQKVSETAKILDLTNLLDRKPSQLSGGQRQRVAMGRAIVRHPKAFLMDEPLSNLDAKLRVQMRGEIAQLQRRLGTTTVYVTHDQTEAMTLGDRVVVMYGGIAQQIGTPEELYERPANLFVAGFIGSPAMNFFPARLTAIGLTLPFGEVTLAPEVQGVIAAHPKPENVIVGVRPEHIQDAALIDAYQRIRALTFQVKVNLVESLGADKYLYFTTESPAVHSVQLDELAEVEGESALHENQFVARVPAESKVAIGQSVELAFDTARLAVFDADSGANLTIPHRA
>biolip__8hplC Lpqy-sugabc in state 1
AEIVLDRVTKSYPRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMVFQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQPLSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMNFFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVHFTTEGAGAESAQLAELAADSGAGTNQFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD
>PDB_8hpr_D Lpqy-sugabc in state 4
AEIVLDRVTKSYPDVRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMV
FQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQP
LSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMN
FFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVH
FTFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD
>PDB_8hpr_C Lpqy-sugabc in state 4
AEIVLDRVTKSYPDVRAAVKEFSMTIADGEFIILVGPSGCGKSTTLNMIAGLEEITSGELRIGGERVNEKAPKDRDIAMV
FQSYALYPHMTVRQNIAFPLTLAKVPKAEIAAKVEETAKILDLSELLDRKPGQLSGGQRQRVAMGRAIVRSPKAFLMDQP
LSNLDAKLRVQMRAEISRLQDRLGTTTVYVTHDQTEAMTLGDRVVVMLAGEVQQIGTPDELYSSPANLFVAGFIGSPAMN
FFPATRTDVGVRLPFGEVTLTPHMLDLLDKQARPENIIVGIRPEHIEDSALLDGYARIRALTFSVRADIVESLGADKYVH
FTTFIARVSADSRVRTGEQIELAIDTTKLSIFDAATGLNLTRD