test.seq

>gi|999613|pdb|1CSX|  Cytochrome C (Isozyme 1) (Reduced) Mutant With Leu 94 Replaced By Ser And Cys 102 Replaced By Thr (L94s,C102t)
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPKKYI
PGTKMAFGGLKKEKDRNDSITYLKKATE
>gi|1127276|pdb|1CTE|B Chain B, Molecule: Cathepsin B; Ec: 3.4.22.1; Mutation: Ser115ala; Engineered; Heterogen: Pyridyl Sulfide Blocking Group At Active-Site Cys 29 >gi|1127275|pdb|1CTE|A Chain A, Molecule: Cathepsin B; Ec: 3.4.22.1; Mutation: Ser115ala; Engineered; Heterogen: Pyridyl Sulfide Blocking Group At Active-Site Cys 29
LPESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGGYPSGAW
NFWTRKGLVSGGVYNSHIGCLPYTIPPCEHHVNGARPPCTGEGDTPKCNKMCEAGYSTSYKEDKHYGYTSYSVSDSEKEI
MAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNADWGDNGFFKILRGENHC
GIESEIVAGIPRTQ
>gi|493956|pdb|1CTP|E Chain E, Camp-Dependent Protein Kinase (E.C.2.7.1.37) (Capk) (Catalytic Subunit)
GNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHFAMKILDKQKVV
KLKQIEHTLNEKRILQAVNFPFLVKLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSL
DLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA
DQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKG
PGDTSNFDDYEEEEIRVSINEKCGKEFSEF
>gi|442771|pdb|1CTZ|  Cytochrome c (Isozyme 1) (Reduced) Mutant With Tyr 67 Replaced By Phe And Cys 102 Replaced By Thr (Y67F, C102T) >gi|442770|pdb|1CTY|   Cytochrome c (Isozyme 1) (Oxidized) Mutant With Tyr 67 Replaced By Phe And Cys 102 Replaced By Thr (Y67F, C102T)
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVLWDENNMSEFLTNPKKYI
PGTKMAFGGLKKEKDRNDLITYLKKATE
>gi|442773|pdb|1CVB|  Carbonic Anhydrase Ii (Hca Ii) (E.C.4.2.1.1) Mutant With Thr 199 Replaced By Val (T199v) (Sulfate-Bound Form) >gi|442772|pdb|1CVA|   Carbonic Anhydrase Ii (Hca Ii) (E.C.4.2.1.1) Mutant With Thr 199 Replaced By Val (T199v) (Azide-Bound Form)
SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKG
GPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVD
VLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLVTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV
DNWRPAQPLKNRQIKASFK
>gi|493958|pdb|1CVC|  Carbonic Anhydrase Ii (E.C.4.2.1.1) Mutant With His 94 Replaced By Asp (H94d)
SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKG
GPLDGTYRLIQFDFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVD
VLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV
DNWRPAQPLKNRQIKASFK
>gi|809316|pdb|1CVD|  Carbonic Anhydrase Ii (Carbonate Dehydratase) (Hca Ii) (E.C.4.2.1.1) Mutant With His 119 Replaced By Cys (H119c)
WGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPL
DGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELCLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLD
SIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNW
RPAQPLKNRQIKASF
>gi|809317|pdb|1CVE|  Carbonic Anhydrase Ii (Carbonate Dehydratase)(Hca Ii) (E.C.4.2.1.1) Mutant With His 119 Replaced By Asp (H119d)
SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKG
GPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELDLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVD
VLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV
DNWRPAQPLKNRQIKASFK
>gi|809318|pdb|1CVF|  Carbonic Anhydrase Ii (Carbonate Dehydratase)(Hca Ii) (E.C.4.2.1.1) Mutant With His 94 Replaced By Ala (H94a)
SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKG
GPLDGTYRLIQFAFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVD
VLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV
DNWRPAQPLKNRQIKASFK
>gi|999651|pdb|1CVH|  Carbonic Anhydrase Ii (Carbonate Dehydratase Ii, Hca Ii) (E.C.4.2.1.1) Mutant With His 96 Replaced By Cys (H96c)
WGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPL
DGTYRLIQFHFCWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLD
SIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNW
RPAQPLKNRQIKASF
>gi|999670|pdb|1CYE|  Chey Mutant With Met 1 Deleted, Arg 1 Inserted, And Ala 2 Replaced By Ser (Del(M1),Ins(R1),A2s) (Nmr, 20 Structures)
RSDKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSA
LPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM
>gi|1311049|pdb|1CYF|  Mol_id: 1; Molecule: Cytochrome C Peroxidase; Chain: Null; Ec: 1.11.1.5; Engineered: Yes; Mutation: Ins(Met Ile At N-Terminus), C128a, A193c
MITTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWDKHDNTGGSYGGTYRFKKEFN
DPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRAGRVDTPEDTTPDNGRLPDADKDAGYVRTFF
QRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGCANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSL
IQDPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL
>gi|349869|pdb|1D66|B Chain B, Gal4 (Residues 1 - 65) Complex With 19mer Dna >gi|349868|pdb|1D66|A Chain A, Gal4 (Residues 1 - 65) Complex With 19mer Dna
MKLLSSIEQACDICRLKKLKCSKEKPKCAKCLKNNWECRYSPKTKRSPLTRAHLTEVESRLERLEF
>gi|576079|pdb|1DBP|  D-Ribose-Binding Protein Mutant With Gly 72 Replaced By Asp (G72d)
KDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVDNAVKMANQ
ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFNVLASQ
PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQI
GAKGVETADKVLKGEKVQAKYPVDLKLVVKQ
>gi|442827|pdb|1DCB|  Carbonic Anhydrase II (Carbonate Dehydratase) (HCA II) (E.C.4.2.1.1) Mutant With Thr 199 Replaced By Cys (T199C) >gi|442826|pdb|1DCA|   Carbonic Anhydrase II (Carbonate Dehydratase) (HCA II) (E.C.4.2.1.1) Mutant With Thr 199 Replaced By Cys (T199C)
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLCTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
>gi|576084|pdb|1DGC|A Chain A, Gcn4 Leucine Zipper Complexed With Specific AtfCREB SITE DNA
IVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER
>gi|640360|pdb|1DGE|  Dialkylglycine Decarboxylase (Pyruvate) (Dgd) (E.C.4.1.1.64) Mutant With Gln 15 Replaced By His (Q15h) Complexed With Rubidium+ In Metal-Binding Sites I And 2 >gi|640359|pdb|1DGD|   Dialkylglycine Decarboxylase (Pyruvate) (Dgd) (E.C.4.1.1.64) Mutant With Gln 15 Replaced By His (Q15h) Complexed With Lithium+ In Metal-Binding Site 1
SLNDDATFWRNARHHLVRYGGTFEPMIIERAKGSFVYDADGRAILDFTSGQMSAVLGHCHPEIVSVIGEYAGKLDHLFSG
MLSRPVVDLATRLANITPPGLDRALLLSTGAESNEAAIRMAKLVTGKYEIVGFAQSWHGMTGAAASATYSAGRKGVGPAA
VGSFAIPAPFTYRPRFERNGAYDYLAELDYAFDLIDRQSSGNLAAFIAEPILSSGGIIELPDGYMAALKRKCEARGMLLI
LDEAQTGVGRTGTMFACQRDGVTPDILTLSKTLGAGLPLAAIVTSAAIEERAHELGYLFYTTHVSDPLPAAVGLRVLDVV
QRDGLVARANVMGDRLRRGLLDLMERFDCIGDVRGRGLLLGVEIVKDRRTKEPADGLGAKITRECMNLGLSMNIVQLPGM
GGVFRIAPPLTVSEDEIDLGLSLLGQAIERAL
>gi|493971|pdb|1DHI|B Chain B, Dihydrofolate Reductase (Dhfr) (E.C.1.5.1.3) Mutant With Asp 27 Replaced By Ser (D27s) Complexed With Methotrexate >gi|493970|pdb|1DHI|A Chain A, Dihydrofolate Reductase (Dhfr) (E.C.1.5.1.3) Mutant With Asp 27 Replaced By Ser (D27s) Complexed With Methotrexate
MISLIAALAVDRVIGMENAMPWNLPASLAWFKRNTLDKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDE
AIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR
>gi|493973|pdb|1DHJ|B Chain B, Dihydrofolate Reductase (Dhfr) (E.C.1.5.1.3) Mutant With Asp 27 Replaced By Ser And Phe 137 Replaced By Ser (D27s,F137s) Complexed With Methotrexate >gi|493972|pdb|1DHJ|A Chain A, Dihydrofolate Reductase (Dhfr) (E.C.1.5.1.3) Mutant With Asp 27 Replaced By Ser And Phe 137 Replaced By Ser (D27s,F137s) Complexed With Methotrexate
MISLIAALAVDRVIGMENAMPWNLPASLAWFKRNTLDKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDE
AIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVSSEFHDADAQNSHSYCFEILERR
>gi|515113|pdb|1DLA|D Chain D, Aldose Reductase (E.C.1.1.1.21) >gi|515112|pdb|1DLA|C Chain C, Aldose Reductase (E.C.1.1.1.21) >gi|515111|pdb|1DLA|B Chain B, Aldose Reductase (E.C.1.1.1.21) >gi|515110|pdb|1DLA|A Chain A, Aldose Reductase (E.C.1.1.1.21)
SHLVLYTGAKMPILGLGTWKSPPGKVTEAVKVAIDLGYRHIDCAHVYQNENEVGLGLQEKLQGQVVKREDLFIVSKLWCT
DHEKNLVKGACQTTLRDLKLDYLDLYLIHWPTGFKPGKDPFPLDGDGNVVPDESDFVETWEAMEELVDEGLVKAIGVSNF
NHLQVEKILNKPGLKYKPAVNQIEVHPYLTQEKLIEYCKSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKYN
KTTAQVLIRFPMQRNLIVIPKSVTPERIAENFQVFDFELSPEDMNTLLSYNRNWRVCALMSCASHKDYPFHEEY
>gi|640362|pdb|1DLC|  Delta-Endotoxin Cryiiia (Bt13)
TTKDVIQKGISVVGDLLGVVGFPFGGALVSFYTNFLNTIWPSEDPWKAFMEQVEALMDQKIADYAKNKALAELQGLQNNV
EDYVSALSSWQKNPVSSRNPHSQGRIRELFSQAESHFRNSMPSFAISGYEVLFLTTYAQAANTHLFLLKDAQIYGEEWGY
EKEDIAEFYKRQLKLTQEYTDHCVKWYNVGLDKLRGSSYESWVNFNRYRREMTLTVLDLIALFPLYDVRLYPKEVKTELT
RDVLTDPIVGVNNLRGYGTTFSNIENYIRKPHLFDYLHRIQFHTRFQPGYYGNDSFNYWSGNYVSTRPSIGSNDIITSPF
YGNKSSEPVQNLEFNGEKVYRAVANTNLAVWPSAVYSGVTKVEFSQYNDQTDEASTQTYDSKRNVGAVSWDSIDQLPPET
TDEPLEKGYSHQLNYVMCFLMQGSRGTIPVLTWTHKSVDFFNMIDSKKITQLPLVKAYKLQSGASVVAGPRFTGGDIIQC
TENGSAATIYVTPDVSYSQKYRARIHYASTSQITFTLSLDGAPFNQYYFDKTINKGDTLTYNSFNLASFSTPFELSGNNL
QIGVTGLSAGDKVYIDKIEFIPVN
>gi|1065363|pdb|1DLR|  Dihydrofolate Reductase (E.C.1.5.1.3) (Dhfr) Mutant With Leu 22 Replaced By Phe (L22f) Complexed With Nadph And Piritrexim (Ptx)
VGSLNCIVAVSQNMGIGKNGDFPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELK
EPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLP
EYPGVLSDVQEEKGIKYKFEVYEKND
>gi|1065364|pdb|1DLS|  Dihydrofolate Reductase (E.C.1.5.1.3) (Dhfr) Mutant With Leu 22 Replaced By Tyr (L22y) Complexed With Nadph And Methotrexate
VGSLNCIVAVSQNMGIGKNGDYPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELK
EPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLP
EYPGVLSDVQEEKGIKYKFEVYEKND
>gi|999988|pdb|1DMD|  Cd-6 Metallothionein-1 (Cd-6 Mt) (Alpha Domain) (Nmr, 18 Structures) >gi|999987|pdb|1DMC|   Cd-6 Metallothionein-1 (Cd-6 Mt) (Alpha Domain) (Nmr, Minimized Average Structure)
SPCQKCTSGCKCATKEECSKTCTKPCSCCPK
>gi|1420988|pdb|1DMF|  Cd-6 Metallothionein-1 (Cd-6 Mt) (Beta Domain) (Nmr, 18 Structures) >gi|1420985|pdb|1DME|   Cd-6 Metallothionein-1 (Cd-6 Mt) (Beta Domain) (Nmr, Minimized Average Structure)
XGPCCNDKCVCQEGGCKAGCQCTSCRCS
>gi|809349|pdb|1DOB|  P-Hydroxybenzoate Hydroxylase Mutant With Tyr 222 Replaced By Phe (Y222f) Complexed With 4-Hydroxybenzoate
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYFVQVPLSEKVEDWSDERFW
TELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
>gi|1064951|pdb|1DPB|  Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Mutant With His 610 Replaced By Cys (H610c)
IPPIPPVDFAKYGEIEEVPMTRLMQIGATNLHRSWLNVPHVTQFESADITELEAFRVAQKAVAEKAGVKLTVLPLLLKAC
AYLLKELPDFNSSLAPSGQALIRKKYVHIGFAVDTPDGLLVPVIRNVDQKSLLQLAAEAAELAEKARSKKLGADAMQGAC
FTISSLGHIGGTAFTPIVNAPEVAILGVSKASMQPVWDGKAFQPRLMLPLSLSYDCRVINGAAAARFTKRLGDLLADIRA
ILL
>gi|1064952|pdb|1DPC|  Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Mutant With Asn 614 Replaced By Asp (N614d)
IPPIPPVDFAKYGEIEEVPMTRLMQIGATNLHRSWLNVPHVTQFESADITELEAFRVAQKAVAEKAGVKLTVLPLLLKAC
AYLLKELPDFNSSLAPSGQALIRKKYVHIGFAVDTPDGLLVPVIRNVDQKSLLQLAAEAAELAEKARSKKLGADAMQGAC
FTISSLGHIGGTAFTPIVNAPEVAILGVSKASMQPVWDGKAFQPRLMLPLSLSYDHRVIDGAAAARFTKRLGDLLADIRA
ILL
>gi|1064957|pdb|1DPD|  Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Mutant With Ser 558 Replaced By Ala (S558a)
IPPIPPVDFAKYGEIEEVPMTRLMQIGATNLHRSWLNVPHVTQFESADITELEAFRVAQKAVAEKAGVKLTVLPLLLKAC
AYLLKELPDFNSSLAPSGQALIRKKYVHIGFAVDTPDGLLVPVIRNVDQKSLLQLAAEAAELAEKARSKKLGADAMQGAC
FTIASLGHIGGTAFTPIVNAPEVAILGVSKASMQPVWDGKAFQPRLMLPLSLSYDHRVINGAAAARFTKRLGDLLADIRA
ILL
>gi|229913|pdb|1FDH|G Chain G, Hemoglobin (Deoxy, Human Fetal FII)
XGHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDAIKHLD
DLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTGVASALSSRYH
>gi|229914|pdb|1FDL|L Chain L, IgG1 Fab Fragment (Anti-Lysozyme Antibody D1.3, Kappa) - Lysozyme (E.C.3.2.1.17) Complex
DIQMTQSPASLSASVGETVTITCRASGNIHNYLAWYQQKQGKSPQLLVYYTTTLADGVPSRFSGSGSGTQYSLKINSLQP
EDFGSYYCQHFWSTPRTFGGGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVL
NSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>gi|494017|pdb|1FGV|L Chain L, Fv Fragment Of A Humanized Version Of The Anti-Cd18 Antibody 'h52' (Huh52-Aa Fv)
DIQMTQSPSSLSASVGDRVTITCRASQDINNYLNWYQQKPGKAPKLLIYYTSTLESGVPSRFSGSGSGTDYTLTISSLQP
EDFATYYCQQGNTLPPTFGAGTKVEIKRT
>gi|494018|pdb|1FGV|H Chain H, Fv Fragment Of A Humanized Version Of The Anti-Cd18 Antibody 'h52' (Huh52-Aa Fv)
EVQLVESGGGLVQPGGSLRLSCATSGYTFTEYTMHWMRQAPGKGLEWVAGINPKNGGTSYADSVKGRFTISVDKSKNTLY
LQMNSLRAEDTAVYYCARWRGLNYGFDVRYFDVWGQGTLVTVSS
>gi|1127150|pdb|1FHB|  Mol_id: 1; Molecule: Ferricytochrome C; Chain: Null; Synonym: Met80ala-Iso-1-Ferricytochrome C (Isozyme 1); Engineered: Yes; Mutation: H39q, M80a, C102s; Heterogen: Cyanide Ion; Other_details: Cyanide Adduct Of Ala 80, Isozyme 1, Oxidized Form
TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRQSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPKKYI
PGTKAAFGGLKKEKDRNDLITYLKKASE
>gi|576107|pdb|1FIG|L Chain L, Immunoglobulin G1 (Kappa Light Chain) Fab' Fragment
ENVLTQSPAIMSASPGEKVTMACRASSSVSSTYLHWYQQKSGASPKLLIYSTSNLASGVPARFSGSGSGTSYSLTISSVE
AEDAATYYCQQYSGYPLTFGAGTKLELKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGV
LNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>gi|576108|pdb|1FIG|H Chain H, Immunoglobulin G1 (Kappa Light Chain) Fab' Fragment
DVQLQQSGPELEKPGASVKISCKASGFSLPGHNINWIVQRNGKSLEWIGNIDPYYGGTNFNPKFKGKATLTVDKSSSTLY
MHLTSLQSEDSAVYYCARRRDGNYGFTYWGQGTLVTVSAAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTW
NSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKI
>gi|999792|pdb|1FIP|B Chain B, Fis Protein (Factor For Inversion Stimulation) Mutant With Pro 61 Replaced By Ala (P61a) >gi|999791|pdb|1FIP|A Chain A, Fis Protein (Factor For Inversion Stimulation) Mutant With Pro 61 Replaced By Ala (P61a)
MFEQRVNSDVLTVSTVNSQDQVTQKPLRDSVKQALKNYFAQLNGQDVNDLYELVLAEVEQALLDMVMQYTRGNQTRAALM
MGINRGTLRKKLKKYGMN
>gi|1421277|pdb|1FNA|  Fibronectin Cell-Adhesion Module Type Iii-10
GSLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASS
KPISINYRTEX
>gi|640406|pdb|1FOR|L Chain L, Igg2a Fab Fragment (Fab17-Ia) (Orthorhombic Crystal Form)
QIVLTQSPAIMSAFPGEKVTITCSATSSVNYMHWFQQKPGTSPKLWIYSSSNLASGVPARFSGSGSGTSYSLTISRMEAE
DAATYYCQQRSSYPITFGSGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLN
SWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>gi|494030|pdb|1FPH|F Chain F, Alpha-Thrombin (E.C.3.4.21.5) Ternary Complex With Hirudin And Fibrinopeptide A
XDFLAEGGGVRX
>gi|1065289|pdb|1FPS|  Avian Farnesyl Diphosphate Synthase (Fps) (E.C.2.5.1.10)
SPVVVEREREEFVGFFPQIVRDLTEDGIGHPEVGDAVARLKEVLQYNAPGGKCNRGLTVVAAYRELSGPGQKDAESLRCA
LAVGWCIELFQAFFLVADDIMDQSLTRRGQLCWYKKEGVGLDAINDSFLLESSVYRVLKKYCRQRPYYVHLLELFLQTAY
QTELGQMLDLITAPVSKVDLSHFSEERYKAIVKYKTAFYSFYLPVAAAMYMVGIDSKEEHENAKAILLEMGEYFQIQDDY
LDCFGDPALTGKVGTDIQDNKCSWLVVQCLQRVTPEQRQLLEDNYGRKEPEKVAKVKELYEAVGMRAAFQQYEESSYRRL
QELIEKHSNRLPKEIFLGLAQKIYKRQK
>gi|576112|pdb|1FRD|  Heterocyst [2fe-2s] Ferredoxin (Oxidized, Recombinant Form)
ASYQVRLINKKQDIDTTIEIDEETTILDGAEENGIELPFSCHSGSCSSCVGKVVEGEVDQSDQIFLDDEQMGKGFALLCV
TYPRSNCTIKTHQEPYLA
>gi|576113|pdb|1FRG|L Chain L, Igg2a Fab Fragment (Fab 269) COMPLEXED WITH INFLUENZA Hemagglutinin Ha1 (Strain X47) (Residues 101 - 108)
DIVMTQSPSSLTVTAGEKVTMSCKSSQSLFNSGKRKNFLTWYHQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLT
ITSVQAEDLAIYYCQNDYSHPLTFGAGTKLELKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSE
RQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>gi|576114|pdb|1FRG|H Chain H, Igg2a Fab Fragment (Fab 269) COMPLEXED WITH INFLUENZA Hemagglutinin Ha1 (Strain X47) (Residues 101 - 108)
EVLLVESGGDLVKPGGFLKLSCAASGFTFSSFGMSWVRHTPDKRLEWVATISNGGGYTYYQDSVKGRFTISRDNAKNTLF
LEMTSLKSEDAGLYYCARRERYDEKGFAYWGRGTLVTVSAAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLT
WNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
>gi|576115|pdb|1FRG|P Chain P, Igg2a Fab Fragment (Fab 269) COMPLEXED WITH INFLUENZA Hemagglutinin Ha1 (Strain X47) (Residues 101 - 108)
XDVPDYASLX
>gi|640408|pdb|1FRH|  Ferredoxin (Fdi) Mutant With Phe 2 Replaced By Tyr (F2y)
AYVVTDNCIKCKYTDCVEVCPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEVPEDMQEFIQLNAELAEVWPN
ITEKKDPLPDAEDWDGVKGKLQHLER
>gi|640409|pdb|1FRI|  Ferredoxin (Fdi) Mutant With Asp 23 Replaced By Asn (D23n)
AFVVTDNCIKCKYTDCVEVCPVNCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEVPEDMQEFIQLNAELAEVWPN
ITEKKDPLPDAEDWDGVKGKLQHLER
>gi|640411|pdb|1FRJ|  Ferredoxin (Fdi) Mutant With Phe 25 Replaced By Ile (F25i)
AFVVTDNCIKCKYTDCVEVCPVDCIYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEVPEDMQEFIQLNAELAEVWPN
ITEKKDPLPDAEDWDGVKGKLQHLER
>gi|640412|pdb|1FRK|  Ferredoxin (Fdi) Mutant With His 35 Replaced By Asp (H35d)
AFVVTDNCIKCKYTDCVEVCPVDCFYEGPNFLVIDPDECIDCALCEPECPAQAIFSEDEVPEDMQEFIQLNAELAEVWPN
ITEKKDPLPDAEDWDGVKGKLQHLER
>gi|640413|pdb|1FRL|  Ferredoxin (Fdi) Mutant With Glu 38 Replaced By Ser (E38s)
AFVVTDNCIKCKYTDCVEVCPVDCFYEGPNFLVIHPDSCIDCALCEPECPAQAIFSEDEVPEDMQEFIQLNAELAEVWPN
ITEKKDPLPDAEDWDGVKGKLQHLER
>gi|640414|pdb|1FRM|  Ferredoxin (Fdi) Mutant With Glu 46 Replaced By Ala (E46a)
AFVVTDNCIKCKYTDCVEVCPVDCFYEGPNFLVIHPDECIDCALCAPECPAQAIFSEDEVPEDMQEFIQLNAELAEVWPN
ITEKKDPLPDAEDWDGVKGKLQHLER
>gi|1065318|pdb|1FRN|  Ferredoxin: Nadp+ Oxidoreductase (Ferredoxin Reductase) (E.C.1.18.1.2) Mutant With Ser 96 Replaced By Val And Recombinant Variant With Phe As Residue 269 (S96v,269f)
QIASDVEAPPPAPAKVEKHSKKMEEGITVNKFKPKTPYVGRCLLNTKITGDDAPGETWHMVFSHEGEIPYREGQSVGVIP
DGEDKNGKPHKLRLYVIASSALGDFGDAKSVSLCVKRLIYTNDAGETIKGVCSNFLCDLKPGAEVKLTGPVGKEMLMPKD
PNATIIMLGTGTGIAPFRSFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPDNFRLDFAVSREQTNE
KGEKMYIQTRMAQYAVELWEMLKKDNTYFYMCGLKGMEKGIDDIMVSLAAAEGIDWIEYKRQLKKAEQWNVEVY
>gi|809402|pdb|1FRP|B Chain B, Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1-Phosphohydrolase) (E.C.3.1.3.11) Complexed With Fructose-2,6-Bisphosphate, Adenosine Monophosphate (Amp), And Zinc >gi|809401|pdb|1FRP|A Chain A, Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1-Phosphohydrolase) (E.C.3.1.3.11) Complexed With Fructose-2,6-Bisphosphate, Adenosine Monophosphate (Amp), And Zinc
TDQAAFDTNIVTLTRFVMEQGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYGIAGATNVTGDQVKKLDVLSNDL
VINVLKSSFATCVLVTEEDKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGRNLV
AAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRNVKIKKKGSIYSINEGYAKEFDPAITEYIQRKKFPPDNSAPY
GARYVGSMVADVHRTLVYGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVPTDIHQRAPIILGS
PEDVTELLEIYQKHA
>gi|999863|pdb|1FRT|C Chain C, Fc Receptor (Neonatal) Complexed With Fc (Igg) (FcFCRN Complex)
SVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPQVKFNWYVDGVQVHNAKTKPREQQYNSTYRVVSVLTVLHQNWLDGKE
YKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL
DSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSL
>gi|640415|pdb|1FRX|  Ferredoxin (Fdi) Mutant With Cys 20 Replaced By Ser (C20s)
AFVVTDNCIKCKYTDCVEVSPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEVPEDMQEFIQLNAELAEVWPN
ITEKKDPLPDAEDWDGVKGKLQHLER
>gi|1421399|pdb|1FTZ|  Fushi Tarazu Protein (Homeodomain) (Nmr, 20 Structures)
XDSKRTRQTYTRYQTLELEKEFHFNRYITRRRRIDIANALSLSERQIKIWFQNRRMKSKKDRTLDSSPEH
>gi|442922|pdb|1FVD|D Chain D, Fab Fragment Of Humanized Antibody 4d5, Version 4 >gi|442920|pdb|1FVD|B Chain B, Fab Fragment Of Humanized Antibody 4d5, Version 4
EVQLVESGGGLVQPGGSLRLSCAASGFNIKDTYIHWVRQAPGKGLEWVARIYPTNGYTRYADSVKGRFTISADTSKNTLY
LQMNSLRAEDTAVYYCSRWGGDGFYAMDVWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVS
WNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
>gi|229926|pdb|1FX1|  Flavodoxin
MPKALIVYGSTTGNTEYTAETIARQLANAGYEVDSRDAASVEAGGLFEGFDLVLLGCSTWGDDSIELQDDFIPLFDSLEE
TGAQGRKVACFGCGDSSYEYFCGAVDAIEEKLKNLGAEIVQDGLRIDGDPRAARDDIVGWAHDVRGAI
>gi|1421429|pdb|1GAE|P Chain P, Mol_id: 1; Molecule: D-Glyceraldehyde-3-Phosphate Dehydrogenase; Chain: O, P; Ec: 1.2.1.12; Engineered: Yes; Mutation: N313t; Other_details: Holo Form >gi|1421428|pdb|1GAE|O Chain O, Mol_id: 1; Molecule: D-Glyceraldehyde-3-Phosphate Dehydrogenase; Chain: O, P; Ec: 1.2.1.12; Engineered: Yes; Mutation: N313t; Other_details: Holo Form
TIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA
NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKV
INDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV
DLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDTETGYSNK
VLDLIAHISK
>gi|999907|pdb|1GBR|B Chain B, Growth Factor Receptor-Bound Protein 2 (Grb2, N-Terminal Sh3 Domain) Complexed With Sos-A Peptide (Nmr, 29 Structures)
SPLLPKLPPKTYKRE
>gi|576118|pdb|1GCG|  GalactoseGLUCOSE-Binding Protein (Closed, Unliganded Form) >gi|442932|pdb|1GCA|   GlucoseGALACTOSE-Binding Protein Complex With Galactose
ADTRIGVTIYKYDDNFMSVVRKAIEKDGKSAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKA
RGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGVIQGDLIAKHWQANQGWDLNKDGKIQYVLLKGEPGHPDAEARTT
YVVKELNDKGIQTEQLALDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPE
ALALVKSGAMAGTVLNDANNQAKATFDLAKNLAEGKGAADGTSWKIENKIVRVPYVGVDKDNLSEFTQK
>gi|494036|pdb|1GDH|B Chain B, D-Glycerate Dehydrogenase (Apo Form) (E.C.1.1.1.29) >gi|494035|pdb|1GDH|A Chain A, D-Glycerate Dehydrogenase (Apo Form) (E.C.1.1.1.29)
KKKILITWPLPEAAMARARESYDVIAHGDDPKITIDEMIETAKSVDALLITLNEKCRKEVIDRIPENIKCISTYSIGFDH
IDLDACKARGIKVGNAPHGVTVATAEIAMLLLLGSARRAGEGEKMIRTRSWPGWEPLELVGEKLDNKTLGIYGFGSIGQA
LAKRAQGFDMDIDYFDTHRASSSDEASYQATFHDSLDSLLSVSQFFSLNAPSTPETRYFFNKATIKSLPQGAIVVNTARG
DLVDNELVVAALEAGRLAYAGFDVFAGEPNINEGYYDLPNTFLFPHIGSAATQAREDMAHQANDLIDALFGGADMSYALA
>gi|809425|pdb|1GEU|B Chain B, Glutathione Reductase (E.C.1.6.4.2) Nad Mutant With Ala 179 Replaced By Gly, Ala 183 By Gly, Val 197 By Glu, Arg 198 By Met, Lys 199 By Phe, His 200 By Asp, And Arg 204 By Phe (A179g,A183g,V197e,R198m,K199f,H200d,R204p) Complexed With Nad And Fad >gi|809424|pdb|1GEU|A Chain A, Glutathione Reductase (E.C.1.6.4.2) Nad Mutant With Ala 179 Replaced By Gly, Ala 183 By Gly, Val 197 By Glu, Arg 198 By Met, Lys 199 By Phe, His 200 By Asp, And Arg 204 By Phe (A179g,A183g,V197e,R198m,K199f,H200d,R204p) Complexed With Nad And Fad >gi|809421|pdb|1GES|B Chain B, Glutathione Reductase (E.C.1.6.4.2) Nad Mutant With Ala 179 Replaced By Gly, Ala 183 By Gly, Val 197 By Glu, Arg 198 By Met, Lys 199 By Phe, His 200 By Asp, And Arg 204 By Phe (A179g,A183g,V197e,R198m,K199f,H200d,R204p) Complexed With Nad >gi|809420|pdb|1GES|A Chain A, Glutathione Reductase (E.C.1.6.4.2) Nad Mutant With Ala 179 Replaced By Gly, Ala 183 By Gly, Val 197 By Glu, Arg 198 By Met, Lys 199 By Phe, His 200 By Asp, And Arg 204 By Phe (A179g,A183g,V197e,R198m,K199f,H200d,R204p) Complexed With Nad
MTKHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHMYGPDYGFDTTINKFN
WETLIASRTAYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPDIPGVEYGIDSDGF
FALPALPERVAVVGAGYIGVELGGVINGLGAKTHLFEMFDAPLPSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTDG
SLTLELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRR
LSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEE
KIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR
>gi|1421556|pdb|1GFF|1 Chain 1, Mol_id: 1; Molecule: Bacteriophage G4 Capsid Proteins Gpf, Gpg, Gpj; Chain: 1, 2, 3; Mutation: Am(E)w4
SNVQTSADRVPHDLSHLVFEAGKIGRLKTISWTPVVAGDSFECDMVGAIRLSPLRRGLAVDSRVDIFSFYIPHRHIYGQQ
WINFMKDGVNASPLPPVTCSSGWDSAAYLGTIPSSTLKVPKFLHQGYLNIYNNYFKPPWSDDLTYANPSNMPSEDYKWGV
RVANLKSIWTAPLPPDTRTSENMTTGTSTIDIMGLQAAYAKLHTEQERDYFMTRYRDIMKEFGGHTSYDGDNRPLLLMRS
EFWASGYDVDGTDQSSLGQFSGRVQQTFNHKVPRFYVPEHGVIMTLAVTRFPPTHEMEMHYLVGKENLTYTDIACDPALM
ANLPPREVSLKEFFHSSPDSAKFKIAEGQWYRTQPDRVAFPYNALDGFPFYSALPSTDLKDRVLVNTNNYDEIFQSMQLA
HWNMQTKFNINVYRHMPTTRDSIMTS
>gi|442935|pdb|1GGC|L Chain L, Igg2a Fab Fragment (50.1) >gi|442933|pdb|1GGB|L Chain L, Igg2a Fab Fragment (50.1)
DIVLTQSPGSLAVSLGQRATISCRASESVDDDGNSFLHWYQQKPGQPPKLLIYRSSNLISGIPDRFSGSGSRTDFTLTIN
PVEADDVATYYCQQSNEDPLTFGAGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQ
NGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>gi|442936|pdb|1GGC|H Chain H, Igg2a Fab Fragment (50.1) >gi|442934|pdb|1GGB|H Chain H, Igg2a Fab Fragment (50.1)
QVQLQESGPGILQPSQTLSLTCSFSGFSLSTYGMGVSWIRQPSGKGLEWLAHIFWDGDKRYNPSLKSRLKISKDTSNNQV
FLKITSVDTADTATYYCVQEGYIYWGQGTSVTVSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGS
LSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
>gi|442940|pdb|1GGI|M Chain M, Igg2a Fab Fragment (50.1) Complex With 16-Residue Peptide (Residues 311-328 Of Hiv-1 Gp120 (Mn Isolate)) >gi|442937|pdb|1GGI|L Chain L, Igg2a Fab Fragment (50.1) Complex With 16-Residue Peptide (Residues 311-328 Of Hiv-1 Gp120 (Mn Isolate))
DIVLTQSPGSLAVSLGQRATISCRASESVDDDGNSFLHWYQQKPGQPPKLLIYRSSNLISGIPDRFSGSGSRTDFTLTIN
PVEADDVATYYCQQSNEDPLTFGAGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQ
NGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>gi|442941|pdb|1GGI|J Chain J, Igg2a Fab Fragment (50.1) Complex With 16-Residue Peptide (Residues 311-328 Of Hiv-1 Gp120 (Mn Isolate)) >gi|442938|pdb|1GGI|H Chain H, Igg2a Fab Fragment (50.1) Complex With 16-Residue Peptide (Residues 311-328 Of Hiv-1 Gp120 (Mn Isolate))
QVQLKESGPGILQPSQTLSLTCSFSGFSLSTYGMGVSWIRQPSGKGLEWLAHIFWDGDKRYNPSLKSRLKISKDTSNNQV
FLKITSVDTADTATYYCVQEGYIYWGQGTSVTVSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGS
LSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPC
>gi|640424|pdb|1GHC|  Gh1 (Histone H1, Variant 11l, Globular Domain) (Nmr, 14 Structures)
MAGPSVTELITKAVSASKERKGLSLAALKKALAAGGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFRLSK
>gi|442944|pdb|1GHL|B Chain B, Lysozyme (E.C.3.2.1.17) >gi|442943|pdb|1GHL|A Chain A, Lysozyme (E.C.3.2.1.17)
GKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCHIP
CSALLSSDITASVNCAKKIVSDGNGMNAWVAWRKHCKGTDVNVWIRGCRL
>gi|1000030|pdb|1GIL|  G I Alpha1 (Guanine Nucleotide-Binding Protein G(I), Alpha-1 Subunit) Mutant With Gln 204 Replaced By Leu (Q204l) Complexed With Gtp-Gamma-S And Magnesium
GCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSI
IAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDR
IAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGLRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMN
RMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYT
HFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
>gi|494043|pdb|1GKY|  Guanylate Kinase (E.C.2.7.4.8) Complex With Guanosine Monophosphate
XSRPIVISGPSGTGKSTLLKKLFAEYPDSFGFSVSSTTRTPRAGEVNGKDYNFVSVDEFKSMIKNNEFIEWAQFSGNYYG
STVASVKQVSKSGKTCILDIDMQGVKSVKAIPELNARFLFIAPPSVEDLKKRLEGRGTETEESINKRLSAAQAELAYAET
GAHDKVIVNDDLDKAYKELKDFIFAEK
>gi|494046|pdb|1GLU|B Chain B, Glucocorticoid Receptor (Dna-Binding Domain) Complex With Dna (First Six Residues Are Clonal Linkers) >gi|494045|pdb|1GLU|A Chain A, Glucocorticoid Receptor (Dna-Binding Domain) Complex With Dna (First Six Residues Are Clonal Linkers)
MKPARPCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTK
K
>gi|494047|pdb|1GLV|  Glutathione Synthase (E.C.6.3.2.3) Loopless Mutant With Residues 226 - 241 Replaced By Gly-Gly-Gly
MIKLGIVMDPIANINIKKDSSFAMLLEAQRRGYELHYMEMGDLYLINGEARAHTRTLNVKQNYEEWFSFVGEQDLPLADL
DVILMRKDPPFDTEFIYATYILERAEEKGTLIVNKPQSLRDCNEKLFTAWFSDLTPETLVTRNKAQLKAFWEKHSDIILK
PLDGMGGASIFRVKEGDPNLGVIAETLTEHGTRYCMAQNYLPAIKDGDKRVLVVDGEPVPYCLARGGGGEPRPLTESDWK
IARQIGPTLKEKGLIFVGLDIIGDRLTEINVTSPTCIREIEAEFPVSITGMLMDAIEARLQQQ
>gi|640432|pdb|1GNB|  Guanylin (B-Form) (Endogenous Ligand To The Heat Stable Enterotoxin Receptor) (Nmr, 20 Structures) >gi|640431|pdb|1GNA|   Guanylin (A-Form) (Endogenous Ligand To The Heat Stable Enterotoxin Receptor) (Nmr, 20 Structures)
TCEICAYAACTGC
>gi|494049|pdb|1GOA|  Ribonuclease H (E.C.3.1.26.4) Mutant With Gly 80b Inserted Between Gln 80 And Trp 81 (Ins(Q80-G) (G80b Rnase H)
MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALKEHCEVILSTDSQYVRQGITQ
GWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEWVKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV
>gi|494050|pdb|1GOB|  Ribonuclease H (E.C.3.1.26.4) Mutant With Gly 77 Replaced By Ala (G77a) (A77 Rnase H)
MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALKEHCEVILSTDSQYVRQAITQ
WIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEWVKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV
>gi|494051|pdb|1GOC|  Ribonuclease H (E.C.3.1.26.4) Mutant With Gly 77 Replaced By Ala And Gly 80b Inserted Between Gln 80 And Trp 81 (G77a,Ins(Q80-G)) (A77G80B RNASE H)
MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALKEHCEVILSTDSQYVRQAITQ
GWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEWVKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV
>gi|229954|pdb|1GPD|R Chain R, D-Glyceraldehyde-3-Phosphate Dehydrogenase (E.C.1.2.1.12) >gi|229953|pdb|1GPD|G Chain G, D-Glyceraldehyde-3-Phosphate Dehydrogenase (E.C.1.2.1.12)
XSKIGINGFGRIGRLVLRAALSCGAQVVAVNDPFIALEYMVYMFKYDSTHGVFKGEVKMEDGALVVDGKKITVFNEMKPE
NIPWSKAGAEYIVESTGVFTTIEKASAHFKGGAKKVVISAPSADAPMFVCGVNLEKYSKDMTVVSNASCTTNCLAPVAKV
LHENFEIVEGLMTTVHAVTATQKTVDGPSAKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELDGKLTGMAFRVPTPDVSVV
DLTVRLGKECSYDDIKAAMKTASEGPLQGFLGYTEDDVVSSDFIGDNRSSIFDAKAGIQLSKTFVKVVSWYDNEFGYSQR
VIDLLKHMQKVDSA
>gi|576141|pdb|1GPH|4 Chain 4, Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase (E.C.2.4.2.14) >gi|576140|pdb|1GPH|3 Chain 3, Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase (E.C.2.4.2.14) >gi|576139|pdb|1GPH|2 Chain 2, Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase (E.C.2.4.2.14) >gi|576138|pdb|1GPH|1 Chain 1, Glutamine Phosphoribosylpyrophosphate (Prpp) Amidotransferase (E.C.2.4.2.14)
CGVFGIWGHEEAPQITYYGLHSLQHRGQEGAGIVATDGEKLTAHKGQGLITEVFQNGELSKVKGKGAIGHVRYATAGGGG
YENVQPLLFRSQNNGSLALAHNGNLVNATQLKQQLENQGSIFQTSSDTEVLAHLIKRSGHFTLKDQIKNSLSMLKGAYAF
LIMTETEMIVALDPNGLRPLSIGMMGDAYVVASETCAFDVVGATYLREVEPGEMLIINDEGMKSERFSMNINRSICSMEY
IYFSRPDSNIDGINVHSARKNLGKMLAQESAVEADVVTGVPDSSISAAIGYAEATGIPYELGLIKNRYVGRTFIQPSQAL
REQGVRMKLSAVRGVVEGKRVVMVDDSIVRGTTSRRIVTMLREAGATEVHVKISSPPIAHPCFYGIDTSTHEELIASSHS
VDEIRQEIGADTLSFLSVEGLLKGIGRKYDDSNCGQCLACFTGKYPTEIYQDTVLPHVKEAVLTK
>gi|493979|pdb|1DRA|B Chain B, Dihydrofolate Reductase (Dhfr) (E.C.1.5.1.3) Mutant With Asp 27 Replaced By Glu (D27e) >gi|493978|pdb|1DRA|A Chain A, Dihydrofolate Reductase (Dhfr) (E.C.1.5.1.3) Mutant With Asp 27 Replaced By Glu (D27e)
MISLIAALAVDRVIGMENAMPWNLPAELAWFKRNTLDKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDE
AIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR
>gi|493981|pdb|1DRB|B Chain B, Dihydrofolate Reductase (Dhfr) (E.C.1.5.1.3) Mutant With Asp 27 Replaced By Cys (D27c) >gi|493980|pdb|1DRB|A Chain A, Dihydrofolate Reductase (Dhfr) (E.C.1.5.1.3) Mutant With Asp 27 Replaced By Cys (D27c)
MISLIAALAVDRVIGMENAMPWNLPACLAWFKRNTLDKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDE
AIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR
>gi|996104|pdb|1DRJ|  D-Ribose-Binding Protein Mutant With Gly 134 Replaced By Arg (G134r) Complexed With Beta-D-Ribose
KDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ
ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIARTSAARERGEGFQQAVAAHKFNVLASQ
PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQI
GAKGVETADKVLKGEKVQAKYPVDLKLVVKQ
>gi|996108|pdb|1DRK|  D-Ribose-Binding Protein Mutant With Ile 132 Replaced By Thr And Gly 134 Replaced By Ala (I132t,G134a)
KDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQ
ANIPVITLDRQATKGEVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGTAATSAARERGEGFQQAVAAHKFNVLASQ
PADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFDGTPDGEKAVNDGKLAATIAQLPDQI
GAKGVETADKVLKGEKVQAKYPVDLKLVVKQ
>gi|442844|pdb|1DTC|  Acetyl-Delta-Toxin (Acetyl-Delta-Haemolysin) (Nmr, 12 Structures)
XMAQDIISTIGDLVKWIIDTVNKFTKK
>gi|1421644|pdb|1DTK|  Dendrotoxin K (Nmr, 20 Structures)
XAKYCKLPLRIGPCKRKIPSFYYKWKAKQCLPFDYSGCGGNANRFKTIEECRRTCVG
>gi|809357|pdb|1DTP|  Diphtheria Toxin Catalytic Domain (Residues 1 - 190) Complexed With Adenylyl(3'->5')uridine 3'-Monophosphate (Apup)
GADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGV
VKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALS
VELEINFETRGKRGQDAMYEYMAQACAGNR
>gi|1064980|pdb|1DTS|  Dethiobiotin Synthase (E.C.6.3.3.3)
MSKRYFVTGTDTEVGKTVASCALLQAAKAAGYRTAGYKPVASGSEKTPEGLRNSDALALQRNSSLQLDYATVNPYTFAEP
TSPHIISAQEGRPIESLVMSAGLRALEQQADWVLVEGAGGWFTPLSDTFTFADWVTQEQLPVILVVGVKLGCINHAMLTA
QVIQHAGLTLAGWVANDVTPPGKRHAEYMTTLTRMIPAPLLGEIPWLAEAATGKYINLALL
>gi|229891|pdb|1DTX|  Alpha-Dendrotoxin
XPRRKLCILHRNPGRCYDKIPAFYYNQKKKQCERFDWSGCGGNSNRFKTIEECRRTCIG
>gi|1064981|pdb|1DVH|  Cytochrome C553 (Reduced) (Nmr, 36 Structures)
ADGAALYKSCIGCHGADGSKAAMGSAKPVKGQGAEELYKKMKGYADGSYGGERKAMMTNAVKKYSDEELKALADYMSKL
>gi|1421659|pdb|1DVR|B Chain B, Nucleoside Monophosphate Kinase, Myokinase Mol_id: 1; Molecule: Adenylate Kinase; Chain: A, B; Synonym: Atp:amp-Phosphotransferase, Myokinase; Ec: 2.7.4.3; Engineered: Yes; Mutation: D89v, R165i >gi|1421658|pdb|1DVR|A Chain A, Nucleoside Monophosphate Kinase, Myokinase Mol_id: 1; Molecule: Adenylate Kinase; Chain: A, B; Synonym: Atp:amp-Phosphotransferase, Myokinase; Ec: 2.7.4.3; Engineered: Yes; Mutation: D89v, R165i
SSESIRMVLIGPPGAGKGTQAPNLQERFHAAHLATGDMLRSQIAKGTQLGLEAKKIMDQGGLVSDDIMVNMIKDELTNNP
ACKNGFILVGFPRTIPQAEKLDQMLKEQGTPLEKAIELKVDDELLVARITGRLIHPASGRSYHKIFNPPKEDMKDDVTGE
ALVQISDDNADALKKRLAAYHAQTEPIVDFYKKTGIWAGVDASQPPATVWADILNKLGKN
>gi|442856|pdb|1DXV|D Chain D, Hemoglobin (Deoxy) Mutant With Val 1 Replaced By Ala In The Beta Chains (Beta V1a) >gi|442854|pdb|1DXV|B Chain B, Hemoglobin (Deoxy) Mutant With Val 1 Replaced By Ala In The Beta Chains (Beta V1a)
AHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
>gi|442857|pdb|1DYA|  Sgamma97-Beta-Mercaptoethanol Lysozyme (E.C.3.2.1.17) Mutant With Val 131 Replaced By Asp (V131d)
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAADNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
>gi|442858|pdb|1DYB|  Sgamma97-Beta-Mercaptoethanol Lysozyme (E.C.3.2.1.17) Mutant With Val 131 Replaced By Gly (V131g)
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAGNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
>gi|442859|pdb|1DYC|  Lysozyme (E.C.3.2.1.17) Mutant With Val 131 Replaced By Ile (V131i)
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAINLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
>gi|442860|pdb|1DYD|  Sgamma97-Beta-Mercaptoethanol Lysozyme (E.C.3.2.1.17) Mutant With Val 131 Replaced By Leu (V131l)
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAALNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
>gi|442861|pdb|1DYE|  Lysozyme (E.C.3.2.1.17) Mutant With Val 131 Replaced By Ser (V131s)
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAASNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
>gi|442862|pdb|1DYF|  Sgamma97-Beta-Mercaptoethanol Lysozyme (E.C.3.2.1.17) Mutant With Val 131 Replaced By Met (V131m)
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAMNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
>gi|442863|pdb|1DYG|  Sgamma97-Beta-Mercaptoethanol Lysozyme (E.C.3.2.1.17) Mutant With Val 131 Replaced By Glu (V131e)
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAENLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
>gi|999509|pdb|1DYN|B Chain B, Dynamin (Pleckstrin Homology Domain) (Dynph) >gi|999508|pdb|1DYN|A Chain A, Dynamin (Pleckstrin Homology Domain) (Dynph)
MKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFAL
FNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDK
>gi|442869|pdb|1EAF|  Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Complex With Hydrogen Sulfite >gi|442868|pdb|1EAE|   Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Complex With Dihydrolipoamide >gi|442867|pdb|1EAD|   Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Complex With Oxidized Coa >gi|442866|pdb|1EAC|   Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Ternary Complex With Oxidized Coa And Dtt >gi|442865|pdb|1EAB|   Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Ternary Complex With Coa And Lipoamide >gi|442864|pdb|1EAA|   Dihydrolipoyl Transacetylase (E.C.2.3.1.12) (Catalytic Domain (Residues 382-637)) Native Structure
IPPIPPVDFAKYGEIEEVPMTRLMQIGATNLHRSWLNVPHVTQFESADITELEAFRVAQKAVAKKAGVKLTVLPLLLKAC
AYLLKELPDFNSSLAPSGQALIRKKYVHIGFAVDTPDGLLVPVIRNVDQKSLLQLAAEAAELAEKARSKKLGADAMQGAC
FTISSLGHIGGTAFTPIVNAPEVAILGVSKASMQPVWDGKAFQPRLMLPLSLSYDHRVINGAAAARFTKRLGDLLADIRA
ILL
>gi|809360|pdb|1EAP|A Chain A, 17e8 Complexed With Phenyl [1-(1-N-Succinylamino)pentyl] Phosphonate
DIELTQSPSSLSASLGGKVTITCKASQDIKKYIGWYQHKPGKGPRLLIHYTSTLLPGIPSRFRGSGSGRDYSFSISNLEG
GDIATYYCLQYYNLRTFGGGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERAQGVLN
SWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>gi|809361|pdb|1EAP|B Chain B, 17e8 Complexed With Phenyl [1-(1-N-Succinylamino)pentyl] Phosphonate
EVQLQESGTELVKPGASVKISCKASGYISTDHAIHWVKQRPEQGLEWIGYISPGNGDIKYNEKFKVKATLTADQSSSTAY
MQLNSLTSEDSAVYFCKRSYYGSSYVDYWGQGTTLTVSSAKTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTW
NSGGLSSSVHTFPALLQSGLYTMSSSVTVPGGGWPSATVTCSVAHPASSTTVDKKL
>gi|1311034|pdb|1ECM|B Chain B, P-Protein, Chorismate Mutase Domain Mol_id: 1; Molecule: Endo-Oxabicyclic Transition State Analogue; Chain: A, B; Domain: Chorismate Mutase Domain, Residues 1 - 109; Engineered: Yes >gi|1311033|pdb|1ECM|A Chain A, P-Protein, Chorismate Mutase Domain Mol_id: 1; Molecule: Endo-Oxabicyclic Transition State Analogue; Chain: A, B; Domain: Chorismate Mutase Domain, Residues 1 - 109; Engineered: Yes
MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI
IEDSVLTQQALLQQHLNKINPHSARIAFL
>gi|442873|pdb|1EDP|  Endothelin 1 (Et 1) (Nmr, Minimized Best Structure)
CSCSSLMDKECVYFCHL
>gi|1127201|pdb|1EDT|  Endo-Beta-N-Acetylglucosaminidase H, Endo H (E.C.3.2.1.96)
APAPVKQGPTSVAYVEVNNNSMLNVGKYTLADGGGNAFDVAVIFAANINYDTGTKTAYLHFNENVQRVLDNAVTQIRPLQ
QQGIKVLLSVLGNHQGAGFANFPSQQAASAFAKQLSDAVAKYGLDGVDFDDEYAEYGNNGTAQPNDSSFVHLVTALRANM
PDKIISLYNIGPAASRLSYGGVDVSDKFDYAWNPYYGTWQVPGIALPKAQLSPAAVEIGRTSRSTVADLARRTVDEGYGV
YLTYNLDGGDRTADVSAFTRELYGSEAVRTP
>gi|999554|pdb|1EFG|C Chain C, Elongation Factor G Complexed With Guanosine 5'-Diphosphate
XXXXXXXXXXXXXXXXXXXXXXXXXXXX
>gi|640371|pdb|1EFT|  Elongation Factor Tu (Ef-Tu) Complexed With Guanosine-5'-(Beta,Gamma-Imido) Triphosphate (Gdpnp)
AKGEFIRTKPHVNVGTIGHVDHGKTTLTAALTFVTAAENPNVEVKDYGDIDKAPEERARGITINTAHVEYETAKRHYSHV
DCPGHADYIKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFMNKVDMVDDPELLDLVEMEVRDLLNQ
YEFPGDEVPVIRGSALLALEEMHKNPKTKRGENEWVDKIWELLDAIDEYIPTPVRDVDKPFLMPVEDVFTITGRGTVATG
RIERGKVKVGDEVEIVGLAPETRKTVVTGVEMHRKTLQEGIAGDNVGLLLRGVSREEVERGQVLAKPGSITPHTKFEASV
YVLKKEEGGRHTGFFSGYRPQFYFRTTDVTGVVRLPQGVEMVMPGDNVTFTVELIKPVALEEGLRFAIREGGRTVGAGVV
TKILE
>gi|1421137|pdb|1EGR|  Glutaredoxin (Reduced) (Nmr, 20 Structures) >gi|1421133|pdb|1EGO|   Glutaredoxin (Oxidized) (Nmr, 20 Structures)
XQTVIFGRSGCPYCVRAKDLAEKLSNERDDFQYQYVDIRAEGITKEDLQQKAGKPVETVPQIFVDQQHIGGYTDFAAWVK
ENLDA
>gi|1421142|pdb|1EGT|  Egf, Epidermal Growth Factor Mol_id: 1; Molecule: Thrombomodulin; Chain: Null; Domain: Epidermal Growth Factor (Egf) Subdomain, Residues 409 - 426; Engineered: Yes; Mutation: Del(Ile 420)
XPEGYILDDGFCTDIDE
>gi|576100|pdb|1ENC|  Staphylococcal Nuclease (E.C.3.1.31.1) Mutant With Asp 21 Replaced By Glu (D21e) Complexed With A Calcium Ion And The Inhibitor Thymidine 3',5'-Diphosphate
ATSTKKLHKEPATLIKAIDGETVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFDKGQ
RTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSEDNADSGQ
>gi|640374|pdb|1ENH|  Engrailed Homeodomain
RPRTAFSSEQLARLKREFNENRYLTERRRQQLSSELGLNEAQIKIWFQNKRAKI
>gi|640375|pdb|1ENI|  Endonuclease V (E.C.3.1.25.1) Mutant With Arg 3 Replaced By Gln (R3q)
MTQINLTLVSELADQHLMAEYRELPRVFGAVRKHVANGKRVRDFKISPTFILGAGHVTFFYDKLEFLRKRQIELIAECLK
RGFNIKDTTVQDISDIPQEFRGDYIPHEASIAISQARLDEKIAQRPTWYKYYGKAIYA
>gi|640376|pdb|1ENJ|  Endonuclease V (E.C.3.1.25.1) Mutant With Glu 23 Replaced By Gln (E23q)
MTRINLTLVSELADQHLMAEYRQLPRVFGAVRKHVANGKRVRDFKISPTFILGAGHVTFFYDKLEFLRKRQIELIAECLK
RGFNIKDTTVQDISDIPQEFRGDYIPHEASIAISQARLDEKIAQRPTWYKYYGKAIYA
>gi|640377|pdb|1ENK|  Endonuclease V (E.C.3.1.25.1) Mutant With Glu 23 Replaced By Asp (E23d)
MTRINLTLVSELADQHLMAEYRDLPRVFGAVRKHVANGKRVRDFKISPTFILGAGHVTFFYDKLEFLRKRQIELIAECLK
RGFNIKDTTVQDISDIPQEFRGDYIPHEASIAISQARLDEKIAQRPTWYKYYGKAIYA
>gi|576104|pdb|1EPB|B Chain B, Epididymal Retinoic Acid-Binding Protein (Androgen Dependent Secretory Protein) (B-Form) Complexed With Retinoic Acid >gi|576103|pdb|1EPB|A Chain A, Epididymal Retinoic Acid-Binding Protein (Androgen Dependent Secretory Protein) (B-Form) Complexed With Retinoic Acid >gi|576102|pdb|1EPA|B Chain B, Epididymal Retinoic Acid-Binding Protein (Androgen Dependent Secretory Protein) (B-Form) >gi|576101|pdb|1EPA|A Chain A, Epididymal Retinoic Acid-Binding Protein (Androgen Dependent Secretory Protein) (B-Form)
AVVKDFDISKFLGFWYEIAFASKMGTPGLAHKEEKMGAMVVELKENLLALTTTYYSEDHCVLEKVTATEGDGPAKFQVTR
LSGKKEVVVEATDYLTYAIIDITSLVAGAVHRTMKLYSRSLDDNGEALYNFRKITSDHGFSETDLYILKHDLTCVKVLQS
AAES
>gi|809375|pdb|1EPL|I Chain I, Endothia Aspartic Proteinase (Endothiapepsin) (E.C.3.4.23.22) Complexed With Ps1 (Pro Leu Glu Psa Arg Leu)
PLEXRL
>gi|809377|pdb|1EPM|I Chain I, Endothia Aspartic Proteinase (Endothiapepsin) (E.C.3.4.23.22) Complexed With Ps2 (Thr Phe Gln Ala Psa Leu Arg Glu)
TFQAXLRE
>gi|999626|pdb|1EPT|A Chain A, Porcine E-Trypsin (E.C.3.4.21.4)
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYK
>gi|999627|pdb|1EPT|B Chain B, Porcine E-Trypsin (E.C.3.4.21.4)
SRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGN
TK
>gi|809387|pdb|1ER8|I Chain I, Endothia Aspartic Proteinase (Endothiapepsin) (E.C.3.4.23.6) Complex With H-77
XPFHLLVY
>gi|515119|pdb|1ERH|  Human Complement Regulatory Protein Cd59 (Extracellular Region, Residues 1 - 70) (Nmr, 10 Structures) >gi|515118|pdb|1ERG|   Human Complement Regulatory Protein Cd59 (Extracellular Region, Residues 1 - 70) (Nmr, Restrained Minimized Average Structure)
LQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLCN
>gi|1431661|pdb|1ERP|  Pheromone Er-10 (Nmr, 20 Structures)
XLCEQSALQCNEQGCHNFCSPEDKPGCLGMVWNPELCP
>gi|515121|pdb|1ESB|  Elastase (E.C.3.4.21.36) Complexed With N-Carbobenzoxy-L-Alanyl-P-Nitrophenol Ester
VVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNNGTEQYVGVQKIVVH
PYWNTDDVAAGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAICSS
SSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN
A
>gi|1311363|pdb|1ESE|  Mol_id: 1; Molecule: Esterase; Chain: Null; Heterogen: Diethyl Phosphonate >gi|1311364|pdb|1ESD|   Mol_id: 1; Molecule: Esterase; Chain: Null; Heterogen: Methyl Phosphonate >gi|1311365|pdb|1ESC|   Mol_id: 1; Molecule: Esterase; Chain: Null
APADPVPTVFFGDSYTANFGIAPVTNQDSERGWCFQAKENYPAVATRSLADKGITLDVQADVSCGGALIHHFWEKQELPF
GAGELPPQQDALKQDTQLTVGSLGGNTLGFNRILKQCSDELRKPSLLPGDPVDGDEPAAKCGEFFGTGDGKQWLDDQFER
VGAELEELLDRIGYFAPDAKRVLVGYPRLVPEDTTKCLTAAPGQTQLPFADIPQDALPVLDQIQKRLNDAMKKAAADGGA
DFVDLYAGTGANTACDGADRGIGGLLEDSQLELLGTKIPWYAHPNDKGRDIQAKQVADKIEEILNR
>gi|229900|pdb|1ETU|  Elongation Factor Tu (Domain I) - Guanosine Diphosphate Complex
XSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAAXXXXXXXXXXXXXXXGITINTSHVEYDTPTRHYAHV
DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ
YDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG
EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRH
TPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG
>gi|442882|pdb|1FAN|  Bovine Pancreatic Trypsin Inhibitor (Bpti) Mutant With Phe 45 Replaced By Ala (F45a)
RPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNAKSAEDCMRTCGGA
>gi|442887|pdb|1FBA|D Chain D, Fructose-1,6-Bisphosphate Aldolase (E.C.4.1.2.13) >gi|442886|pdb|1FBA|C Chain C, Fructose-1,6-Bisphosphate Aldolase (E.C.4.1.2.13) >gi|442885|pdb|1FBA|B Chain B, Fructose-1,6-Bisphosphate Aldolase (E.C.4.1.2.13) >gi|442884|pdb|1FBA|A Chain A, Fructose-1,6-Bisphosphate Aldolase (E.C.4.1.2.13)
XTTYFNYPSKELQDELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTDPKLAENISGVILF
HETLYQKADDGTPFAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPS
YQSILENANVLARYASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQSA
KKNTPEEIALATVQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENI
AAGQNELLKRAKANGDAAQGKYVAGSAGAGSGSLFVANHAY
>gi|999693|pdb|1FBI|P Chain P, Fab Fragment Of The Monoclonal Antibody F9.13.7 (Igg1) Complexed With Lysozyme (E.C.3.2.1.17) >gi|999690|pdb|1FBI|L Chain L, Fab Fragment Of The Monoclonal Antibody F9.13.7 (Igg1) Complexed With Lysozyme (E.C.3.2.1.17)
DIQMTQTTSSLSASLGDRVTISCRASQDISNYLNWYQKKPDGTVKLLIYYTSRLHSGVPSRFSGSGSGTDYSLTIRNLEQ
EDIATYFCQQGYTLPYTFGGGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVL
NSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>gi|999694|pdb|1FBI|Q Chain Q, Fab Fragment Of The Monoclonal Antibody F9.13.7 (Igg1) Complexed With Lysozyme (E.C.3.2.1.17) >gi|999691|pdb|1FBI|H Chain H, Fab Fragment Of The Monoclonal Antibody F9.13.7 (Igg1) Complexed With Lysozyme (E.C.3.2.1.17)
QVQLQQPGAELVKPGASVKLSCKASGYTFTSYWMHWVKQGPGQGLEWIGEIDPSDSYPNYNEKFKGKATLTVDKSSSTAY
MQLSSLTSEDSAVYYCASLYYYGTSYGVLDYWGQGTSVTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVT
VTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVP
>gi|229907|pdb|1FC2|C Chain C, Immunoglobulin Fc And Fragment B Of Protein A Complex
ADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQXXK
>gi|229908|pdb|1FC2|D Chain D, Immunoglobulin Fc And Fragment B Of Protein A Complex >gi|229906|pdb|1FC1|B Chain B, Fc Fragment (Igg1 Class) >gi|229905|pdb|1FC1|A Chain A, Fc Fragment (Igg1 Class)
THTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPQVKFNWYVDGVQVHNAKTKPREQQYNSTYRV
VSVLTVLHQNWLDGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWE
SNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
>gi|1065197|pdb|1FCA|  Ferredoxin
AYVINEACISCGACEPECPVDAISQGGSRYVIDADTCIDCGACAGVCPVDAPVQA
>gi|1065199|pdb|1FCC|A Chain A, Immunoglobin Fc (Igg1) Complexed With Protein G (C2 Fragment)
PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPQVKFNWYVDGVQVHNAKTKPREQQYNSTYRVVSVLTVLHQNWLDGK
EYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPV
LDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSL
>gi|1065200|pdb|1FCC|C Chain C, Immunoglobin Fc (Igg1) Complexed With Protein G (C2 Fragment)
TTYKLVINGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTE
>gi|809395|pdb|1FCD|B Chain B, Flavocytochrome C Sulfide Dehydrogenase (Fcsd) >gi|809393|pdb|1FCD|A Chain A, Flavocytochrome C Sulfide Dehydrogenase (Fcsd)
AGRKVVVVGGGTGGATAAKYIKLADPSIEVTLIEPNTDYYTCYLSNEVIGGDRKLESIKHGYDGLRAHGIQVVHDSATGI
DPDKKLVKTAGGAEFGYDRCVVAPGIELIYDKIEGYSEEAAAKLPHAWKAGEQTAILRKQLEDMADGGTVVIAPPAAPFR
CPPGPYERASQVAYYLKAHKPMSKVIILDSSQTFSKQSQFSKGWERLYGFGTENAMIEWHPGPDSAVVKVDGGEMMVETA
FGDEFKADVINLIPPQRAGKIAQIAGLTNDAGWCPVDIKTFESSIHKGIHVIGDASIANPMPKSGYSANSQGKVAAAAVV
VLLKGEEPGTPSYLNTCYSILAPAYGISVAAIYRPNADGSAIESVPDSGGVTPVDAPDWVLEREVQYAYSWYNNIVHDTF
G
>gi|442900|pdb|1FCS|  Myoglobin Mutant With His 64 Replaced By Val And Thr 67 Replaced By Arg (H64v,T67r)
MVLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKVGVRVLTALGAILKKK
GHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGNFGADAQGAMNKALELFRKDIAAKYKELGYQG
>gi|576106|pdb|1FCT|  Ferredoxin Chloroplastic Transit Peptide Sequence From The Green Alga (Chlamydomonas Reinhardtii) (Nmr, 27 Structures)
MAMAMRSTFAARVGAKPAVRGARPASRMSCMA
>gi|229911|pdb|1FD2|  Ferredoxin (Mutant With Cys 20 Replaced By Ala) (C20A)
AFVVTDNCIKCKYTDCVEVAPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEVPEDMQEFIQLNAELAEVWPN
ITEKKDPLPDAEDWDGVKGKLQHLER
>gi|442904|pdb|1FDD|  Ferredoxin Mutant With Asp 15 Replaced By Asn (D15n)
AFVVTDNCIKCKYTNCVEVCPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEVPEDMQEFIQLNAELAEVWPN
ITEKKDPLPDAEDWDGVKGKLQHLER
>gi|1311356|pdb|1GRL|  Mol_id: 1; Molecule: Groel (Hsp60 Class); Chain: Null; Engineered: Yes; Mutation: R13g, A126v
MAAKDVKFGNDAGVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASK
ANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVTVAVEELKALSVPCSDSKAIAQVGTISANSDETVGK
LIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAV
AKAGKPLLIIAEDVEGEALATAVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQA
KRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDAL
HATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNA
ATEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGGMGGMGGMM
>gi|1421105|pdb|1GRO|  Oxidoreductase, Nadp, Phosphorylation, Glyoxylate Bypass Mol_id: 1; Molecule: Isocitrate Dehydrogenase; Chain: Null; Ec: 1.1.1.42; Engineered: Yes; Mutation: S113e, N115l
MESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQ
DVWLPAETLDLIREYRVAIKGPLTTPVGGGIRELLVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIY
AGIEWKADSADAEKVIKFLREEMGVKKIRFPDHCGIGIKPCSEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGA
FKDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGI
GIAPGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAEMMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGA
KLLKCSEFGDAIIENM
>gi|1421106|pdb|1GRP|  Oxidoreductase, Nadp, Phosphorylation, Glyoxylate Bypass Mol_id: 1; Molecule: Isocitrate Dehydrogenase; Chain: Null; Ec: 1.1.1.42; Mutation: N115l
MESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQ
DVWLPAETLDLIREYRVAIKGPLTTPVGGGIRSLLVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIY
AGIEWKADSADAEKVIKFLREEMGVKKIRFPDHCGIGIKPCSEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGA
FKDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGI
GIAPGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAEMMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGA
KLLKCSEFGDAIIENM
>gi|1065036|pdb|1HAR|  Hiv-1 Reverse Transcriptase (Amino-Terminal Half) (Fingers And Palm Subdomains) (Rt216) (E.C.2.7.7.49)
PISPIETVPVKLKPGMDGPKVAQWPLTAAKIAALVAICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWAKLVDFREL
NKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIF
QSSMTKILAPFKAANPDIVIYQYMDDLYVGSDLAIGAHRTKIEELRQHLLRWGLTT
>gi|494073|pdb|1HBA|D Chain D, Hemoglobin Rothschild (Deoxy) >gi|494071|pdb|1HBA|B Chain B, Hemoglobin Rothschild (Deoxy)
VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPRTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
>gi|494079|pdb|1HBQ|  Retinol Binding Protein (Apo Form) (Apo Brbp)
ERDCRVSSFRVKENFDKARFAGTWYAMAKKDPEGLFLQDNIVAEFSVDENGQMSATAKGRVRLLNNWDVCADMVGTFTDT
EDPAKFKMKYWGVASFLQKGNDDHWIIDTDYETFAVQYSCRLLNLDGTCADSYSFVFARDPSGFSPEVQKIVRQRQEELC
LARQYRLIPHNGYCNGKSERNIL
>gi|809467|pdb|1HCC|  16th Complement Control Protein (CCP) Of Factor H
EGLPCKSPPEISHGVVAHMSDSYQYGEEVTYKCFEGFGIDGPAIAKCLGEKWSHPPSCX
>gi|1065082|pdb|1HCG|B Chain B, Blood Coagulation Factor Xa
CSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLER
>gi|1311090|pdb|1HCP|  Mol_id: 1; Molecule: HumanCHICKEN ESTROGEN RECEPTOR; Chain: Null; Domain: Dna-Binding Domain (Erdbd); Engineered: Yes
MKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGG
>gi|1311087|pdb|1HCQ|F Chain F, Mol_id: 1; Molecule: HumanCHICKEN ESTROGEN RECEPTOR; Chain: A, B, E, F; Domain: Dna-Binding Domain (Erdbd); Engineered: Yes; Mol_id: 2; Molecule: Dna (5'-D(CpCpApGpGpTpCpApCpApGpTpGp ApCpCpTpG)-3') (Dot) Dna (5'-D(CpCpApGpGpTpCpA PCpTpGpTpGpApCpCpTpG)-3'); Chain: C, D, G, H >gi|1311086|pdb|1HCQ|E Chain E, Mol_id: 1; Molecule: HumanCHICKEN ESTROGEN RECEPTOR; Chain: A, B, E, F; Domain: Dna-Binding Domain (Erdbd); Engineered: Yes; Mol_id: 2; Molecule: Dna (5'-D(CpCpApGpGpTpCpApCpApGpTpGp ApCpCpTpG)-3') (Dot) Dna (5'-D(CpCpApGpGpTpCpA PCpTpGpTpGpApCpCpTpG)-3'); Chain: C, D, G, H >gi|1311083|pdb|1HCQ|B Chain B, Mol_id: 1; Molecule: HumanCHICKEN ESTROGEN RECEPTOR; Chain: A, B, E, F; Domain: Dna-Binding Domain (Erdbd); Engineered: Yes; Mol_id: 2; Molecule: Dna (5'-D(CpCpApGpGpTpCpApCpApGpTpGp ApCpCpTpG)-3') (Dot) Dna (5'-D(CpCpApGpGpTpCpA PCpTpGpTpGpApCpCpTpG)-3'); Chain: C, D, G, H >gi|1311082|pdb|1HCQ|A Chain A, Mol_id: 1; Molecule: HumanCHICKEN ESTROGEN RECEPTOR; Chain: A, B, E, F; Domain: Dna-Binding Domain (Erdbd); Engineered: Yes; Mol_id: 2; Molecule: Dna (5'-D(CpCpApGpGpTpCpApCpApGpTpGp ApCpCpTpG)-3') (Dot) Dna (5'-D(CpCpApGpGpTpCpA PCpTpGpTpGpApCpCpTpG)-3'); Chain: C, D, G, H
MKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKD
RRGG
>gi|229971|pdb|1HDD|D Chain D, Engrailed Homeodomain Complex With DNA >gi|229970|pdb|1HDD|C Chain C, Engrailed Homeodomain Complex With DNA
MDEKRPRTAFSSEQLARLKREFNENRYLTERRRQQLSSELGLNEAQIKIWFQNKRAKIKKS
>gi|999603|pdb|1HDP|  Oct-2 Pou Homeodomain (Nmr, Average Structure)
RRKKRTSIETNVRFALEKSFLANQKPTSEEILLIAEQLHMEKEVIRVWFCNRRQKEKRINPCX
>gi|229976|pdb|1HDS|C Chain C, Hemoglobin (Sickle Cell) >gi|229974|pdb|1HDS|A Chain A, Hemoglobin (Sickle Cell)
VLSAANKSNVKAAWGKVGGNAPAYGAQALQRMFLSFPTTKTYFPHFDLSHGSAQQKAHGQKVANALTKAQGHLNDLPGTL
SNLSNLHAHKLRVNPVNFKLLSHSLLVTLASHLPTNFTPAVHANLNKFLANDSTVLTSKYR
>gi|229977|pdb|1HDS|D Chain D, Hemoglobin (Sickle Cell) >gi|229975|pdb|1HDS|B Chain B, Hemoglobin (Sickle Cell)
MLTAEEKAAVTGFWGKVDVDVVGAQALGRLLVVYPWTQRFFQHFGNLSSAGAVMNNPKVKAHGKRVLDAFTQGLKHLDDL
KGAFAQLSGLHCNKLHVNPQNFRLLGNVLALVVARNFGGQFTPNVQALFQKVVAGVANALAHKYH
>gi|1311347|pdb|1HDT|L Chain L, Mol_id: 1; Molecule: Alpha-Thrombin; Chain: L, H; Ec: 3.4.21.5; Mol_id: 2; Molecule: Hirugen Peptide; Chain: P; Engineered: Yes; Mol_id: 3; Molecule: N-[n-[n-[4-(Aminoiminomethyl)amino]-1-Oxobutyl]-L -Phenylalanyl]-L-Allo-Threonyl-L-Phenylalanine, Methyl Ester (Bms-183507); Chain: I; Engineered: Yes
SGEADCGLRPLFEKKSLEDKTERELLESYIDGR
>gi|1311349|pdb|1HDT|P Chain P, Mol_id: 1; Molecule: Alpha-Thrombin; Chain: L, H; Ec: 3.4.21.5; Mol_id: 2; Molecule: Hirugen Peptide; Chain: P; Engineered: Yes; Mol_id: 3; Molecule: N-[n-[n-[4-(Aminoiminomethyl)amino]-1-Oxobutyl]-L -Phenylalanyl]-L-Allo-Threonyl-L-Phenylalanine, Methyl Ester (Bms-183507); Chain: I; Engineered: Yes
XGDFEEIPEEYLQ
>gi|229978|pdb|1HEA|  Carbonic Anhydrase II (Carbonate Dehydratase) (HCA II) (E.C.4.2.1.1) Mutant With Leu 198 Replaced By Arg (L198R)
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSRTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
>gi|229979|pdb|1HEB|  Carbonic Anhydrase II (Carbonate Dehydratase) (HCA II) (E.C.4.2.1.1) Mutant With Leu 198 Replaced By Glu (L198E)
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSETTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
>gi|229980|pdb|1HEC|  Carbonic Anhydrase II (Carbonate Dehydratase) (HCA II) (E.C.4.2.1.1) Mutant With Leu 198 Replaced By His (L198H)
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSHTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
>gi|229981|pdb|1HED|  Carbonic Anhydrase II (Carbonate Dehydratase) (HCA II) (E.C.4.2.1.1) Mutant With Leu 198 Replaced By Ala (L198A)
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSATTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
>gi|576148|pdb|1HEF|I Chain I, Hiv-1 Protease Complexed With Skf 108738 (Hef)
AAFXFVVX
>gi|576149|pdb|1HEG|E Chain E, Hiv-1 Protease Complexed With Skf 107457 (Heg) >gi|576147|pdb|1HEF|E Chain E, Hiv-1 Protease Complexed With Skf 108738 (Hef)
PQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEENSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPT
PVNIIGRNLLTQIGCTLNF
>gi|576150|pdb|1HEG|I Chain I, Hiv-1 Protease Complexed With Skf 107457 (Heg)
AAFXGVVX
>gi|442980|pdb|1HEM|  Lysozyme (E.C.3.2.1.17) Mutant With Ser 91 Replaced By Thr (S91t)
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|442981|pdb|1HEN|  Lysozyme (E.C.3.2.1.17) Mutant With Ile 55 Replaced By Val And Ser 91 Replaced By Thr (I55v,S91t)
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGVLQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|442982|pdb|1HEO|  Lysozyme (E.C.3.2.1.17) Mutant With Ile 55 Replaced By Val (I55v)
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGVLQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|442983|pdb|1HEP|  Lysozyme (E.C.3.2.1.17) Mutant With Thr 40 Replaced By Ser, Ile 55 Replaced By Val, And Ser 91 Replaced By Thr (T40s,I55v,S91t)
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGVLQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|442984|pdb|1HEQ|  Lysozyme (E.C.3.2.1.17) Mutant With Thr 40 Replaced By Ser And Ser 91 Replaced By Thr (T40s,S91t)
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITATVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|442985|pdb|1HER|  Lysozyme (E.C.3.2.1.17) Mutant With Thr 40 Replaced By Ser (T40s)
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNSQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL
>gi|1065143|pdb|1HEY|  Chey Mutant With Asp 12 Replaced By Gly, Asp 13 Replaced By Asn, Phe 14 Replaced By Gly, Ser 15 Replaced By Gly, Met 17 Replaced By Gly, Arg 18 Replaced By Lys, Arg 19 Replaced By Ser, Ile 20 Replaced By Thr, Glu 35 Replaced By Asp (D12g, D13n,F14g,S15g,M17g,R18k,R19s,I20t,E35d) (Synchrotron X-Ray Diffraction)
ADKELKFLVVGNGGTGKSTVRNLLKELGFNNVEDAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSAL
PVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM
>gi|442986|pdb|1HFH|  Factor H, 15th And 16th C-Module Pair (Nmr, Minimized Averaged Structure)
EKIPCSQPPQIEHGTINSSRSSQESYAHGTKLSYTCEGGFRISEENETTCYMGKWSSPPQCEGLPCKSPPEISHGVVAHM
SDSYQYGEEVTYKCFEGFGIDGPAIAKCLGEKWSHPPSCI
>gi|442987|pdb|1HFI|  Factor H, 15th C-Module Pair (Nmr, Minimized Averaged Structure)
EKIPCSQPPQIEHGTINSSRSSQESYAHGTKLSYTCEGGFRISEENETTCYMGKWSSPPQCE
>gi|494152|pdb|1HIB|  Interleukin-1 Beta (Human) Mutant With Thr 9 Replaced By Gly (T9g)
APVRSLNCGLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTL
QLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS
>gi|1431745|pdb|1HIC|  Hirudin Variant 1 (Residues 1 - 51) (Nmr, 20 Structures)
XVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSH
>gi|494160|pdb|1HIM|P Chain P, Igg2a Fab Fragment (Fab 179) COMPLEX WITH PEPTIDE OF Influenza Hemagglutinin Ha1 (Strain X47) (Residues 100-108)
YDVPDYASX
>gi|494163|pdb|1HIM|R Chain R, Igg2a Fab Fragment (Fab 179) COMPLEX WITH PEPTIDE OF Influenza Hemagglutinin Ha1 (Strain X47) (Residues 100-108)
YDVPDYASLX
>gi|494164|pdb|1HIN|L Chain L, Igg2a Fab Fragment (Fab 179) COMPLEXED WITH PEPTIDE OF Influenza Hemagglutinin Ha1 (Strain X47) (Residues 100-107) >gi|494161|pdb|1HIM|J Chain J, Igg2a Fab Fragment (Fab 179) COMPLEX WITH PEPTIDE OF Influenza Hemagglutinin Ha1 (Strain X47) (Residues 100-108) >gi|494158|pdb|1HIM|H Chain H, Igg2a Fab Fragment (Fab 179) COMPLEX WITH PEPTIDE OF Influenza Hemagglutinin Ha1 (Strain X47) (Residues 100-108) >gi|494156|pdb|1HIL|C Chain C, Igg2a Fab Fragment (Fab 179) >gi|494154|pdb|1HIL|A Chain A, Igg2a Fab Fragment (Fab 179)
DIVMTQSPSSLTVTAGEKVTMSCTSSQSLFNSGKQKNYLTWYQQKPGQPPKVLIYWASTRESGVPDRFTGSGSGTDFTLT
ISSVQAEDLAVYYCQNDYSNPLTFGGGTKLELKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSE
RQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>gi|494166|pdb|1HIN|P Chain P, Igg2a Fab Fragment (Fab 179) COMPLEXED WITH PEPTIDE OF Influenza Hemagglutinin Ha1 (Strain X47) (Residues 100-107)
YDVPDYAS
>gi|494168|pdb|1HIQ|B Chain B, Insulin (Human) Mutant With Phe B 24 Replaced By Ser (F24s) (Nmr, Representative Plus 9 Structures)
FVNQHLCGSHLVEALYLVCGERGSFYTPKT
>gi|494172|pdb|1HIT|B Chain B, Insulin (Human) Mutant With Phe B 24 Replaced By Gly (F24g) (Nmr, Representative Plus 8 Structures)
FVNQHLCGSHLVEALYLVCGERGGFYTPKT
>gi|999744|pdb|1HJR|D Chain D, Holliday Junction Resolvase (E.C.3.1.22.4) (Ruvc) >gi|999743|pdb|1HJR|C Chain C, Holliday Junction Resolvase (E.C.3.1.22.4) (Ruvc) >gi|999742|pdb|1HJR|B Chain B, Holliday Junction Resolvase (E.C.3.1.22.4) (Ruvc) >gi|999741|pdb|1HJR|A Chain A, Holliday Junction Resolvase (E.C.3.1.22.4) (Ruvc)
AIILGIDPGSRVTGYGVIRQVGRQLSYLGSGCIRTKVDDLPSRLKLIYAGVTEIITQFQPDYFAIEQVFMAKNADSALKL
GQARGVAIVAAVNQELPVFEYAARQVKQTVVGIGSAEKSQVQHMVRTLLKLPANPQADAADALAIAITHCHVSQNAMQ
>gi|229993|pdb|1HKG|  Hexokinase A And Glucose Complex (E.C.2.7.1.1)
AASXDXSLVEVHXXVFIVPPXILQAVVSIATTRXDDXDSAAASIPMVPGWVLKQVXGSQAGSFLAIVMGGGDLEVILIXL
AGYQESSIXASRSLAASMXTTAIPSDLWGNXAXSNAAFSSXEFSSXAGSVPLGFTFXEAGAKEXVIKGQITXQAXAFSLA
XLXKLISAMXNAXFPAGDXXXXVADIXDSHGILXXVNYTDAXIKMGIIFGSGVNAAYWCDSTXIADAADAGXXGGAGXMX
VCCXQDSFRKAFPSLPQIXYXXTLNXXSPXAXKTFEKNSXAKNXGQSLRDVLMXYKXXGQXHXXXAXDFXAANVENSSYP
AKIQKLPHFDLRXXXDLFXGDQGIAXKTXMKXVVRRXLFLIAAYAFRLVVCXIXAICQKKGYSSGHIAAXGSXRDYSGFS
XNSATXNXNIYGWPQSAXXSKPIXITPAIDGEGAAXXVIXSIASSQXXXAXXSAXXA
>gi|1431789|pdb|1HKT|  Heat Shock Transcription Factor (Nmr, 28 Structures) >gi|1431785|pdb|1HKS|   Heat Shock Transcription Factor (Nmr, Restrained Minimized Average Structure)
XSGVPAFLAKLWRLVDDADTNRLICWTKDGQSFVIQNQAQFAKELLPLNYKHNNMASFIRQLNMYGFHKITSIDNGGLRF
DRDEIEFSHPFFKRNSPFLLDQIKRK
>gi|229995|pdb|1HLA|M Chain M, Human Class I Histocompatibility Antigen A2 (HLA-A2, Human Leucocyte Antigen)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC
RVNHVTLSQPKIVKWDR
>gi|576151|pdb|1HLB|  Hemoglobin (Sea Cucumber)
XGGTLAIQAQGDLTLAQKKIVRKTWHQLMRNKTSFVTDVFIRIFAYDPSAQNKFPQMAGMSASQLRSSRQMQAHAIRVSS
IMSEYVEELDSDILPELLATLARTHDLNKVGADHYNLFAKVLMEALQAELGSDFNEKTRDAWAKAFSVVQAVLLVKHG
>gi|515140|pdb|1HLC|B Chain B, Lectin (Human L-14-Ii) Complexed With Lactose >gi|515139|pdb|1HLC|A Chain A, Lectin (Human L-14-Ii) Complexed With Lactose
ELEVKNMDMKPGSTLKITGSIADGTDGFVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGSEVK
FTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKLKE
>gi|494175|pdb|1HLE|A Chain A, Horse Leukocyte Elastase Inhibitor (Hlei)
XMEQLSTANTHFAVDLFRALNESDPTGNIFISPLSISSALAMIFLGTRGNTAAQVSKALYFDTVEDIHSRFQSLNADINK
PGAPYILKLANRLYGEKTYNFLADFLASTQKMYGAELASVDFQQAPEDARKEINEWVKGQTEGKIPELLVKGMVDNMTKL
VLVNAIYFKGNWQQKFMKEATRDAPFRLNKKDTKTVKMMYQKKKFPYNYIEDLKCRVLELPYQGKELSMIILLPDDIEDE
STGLEKIEKQLTLDKLREWTKPENLYLAEVNVHLPRFKLEESYDLTSHLARLGVQDLFNRGKADLSGMSGARDLFVSKII
HKSFVDLNEEGTEAAAATAGTILLA
>gi|494176|pdb|1HLE|B Chain B, Horse Leukocyte Elastase Inhibitor (Hlei)
EENFNADHPFIFFIRHNPSANILFLGRFSSP
>gi|999806|pdb|1HLM|  Hemoglobin (Cyano-Met) (Sea Cucumber)
XGATQSFQSVGDLTPAEKDLIRSTWDQLMTHRTGFVADVFIRIFHNDPTAQRKFPQMAGLSPAELRTSRQMHAHAIRVSA
LMTTYIDEMDTEVLPELLATLTRTHDKNHVGKKNYDLFGKVLMEAIKAELGVGFTKQVHDAWAKTFAIVQGVLITKHAS
>gi|1421267|pdb|1HMA|  Hmg-D (Hmg-Box Domain, Residues 2 - 74) (Nmr, 20 Structures)
XDKPKRPLSAYMLWLNSARESIKRENPGIKVTEVAKRGGELWRAMKDKSEWEAKAAKAKDDYDRAVKEFEANG
>gi|515142|pdb|1HMC|B Chain B, Human Macrophage Colony Stimulating Factor (Alpha Form, Soluble) >gi|515141|pdb|1HMC|A Chain A, Human Macrophage Colony Stimulating Factor (Alpha Form, Soluble)
SEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQEL
SLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQGH
>gi|576154|pdb|1HMF|  High Mobility Group Protein Fragment-B (Hmgb) (Dna-Binding Hmg-Box Domain B Of Rat Hmg1) (Nmr, 30 Structures) >gi|576153|pdb|1HME|   High Mobility Group Protein Fragment-B (Hmgb) (Dna-Binding Hmg-Box Domain B Of Rat Hmg1) (Nmr, 1 Structure)
FKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAK
>gi|230003|pdb|1HMO|D Chain D, Hemerythrin (Oxy) >gi|230002|pdb|1HMO|C Chain C, Hemerythrin (Oxy) >gi|230001|pdb|1HMO|B Chain B, Hemerythrin (Oxy) >gi|230000|pdb|1HMO|A Chain A, Hemerythrin (Oxy) >gi|229999|pdb|1HMD|D Chain D, Hemerythrin (Deoxy) >gi|229998|pdb|1HMD|C Chain C, Hemerythrin (Deoxy) >gi|229997|pdb|1HMD|B Chain B, Hemerythrin (Deoxy) >gi|229996|pdb|1HMD|A Chain A, Hemerythrin (Deoxy)
GFPIPDPYCWDISFRTFYTIIDDEHKTLFNGILLLSQADNADHLNELRRCTGKHFLNEQQLMQSSQYAGYAEHKKAHDDF
IHKLDTWDGDVTYAKNWLVNHIKTIDFKYRGKI
>gi|494191|pdb|1HNC|D Chain D, Glutathione S-Transferase (Human, Class Mu) (Gstm2-2) Form C (E.C.2.5.1.18) Mutant With Trp 214 Replaced By Phe (W214f) >gi|494190|pdb|1HNC|C Chain C, Glutathione S-Transferase (Human, Class Mu) (Gstm2-2) Form C (E.C.2.5.1.18) Mutant With Trp 214 Replaced By Phe (W214f) >gi|494189|pdb|1HNC|B Chain B, Glutathione S-Transferase (Human, Class Mu) (Gstm2-2) Form C (E.C.2.5.1.18) Mutant With Trp 214 Replaced By Phe (W214f) >gi|494188|pdb|1HNC|A Chain A, Glutathione S-Transferase (Human, Class Mu) (Gstm2-2) Form C (E.C.2.5.1.18) Mutant With Trp 214 Replaced By Phe (W214f) >gi|494187|pdb|1HNB|B Chain B, Glutathione S-Transferase (Human, Class Mu) (Gstm2-2) Form B (E.C.2.5.1.18) Mutant With Trp 214 Replaced By Phe (W214f) >gi|494186|pdb|1HNB|A Chain A, Glutathione S-Transferase (Human, Class Mu) (Gstm2-2) Form B (E.C.2.5.1.18) Mutant With Trp 214 Replaced By Phe (W214f) >gi|494185|pdb|1HNA|   Glutathione S-Transferase (Human, Class Mu) (Gstm2-2) Form A (E.C.2.5.1.18) Mutant With Trp 214 Replaced By Phe (W214f)
PMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGTHKITQSNAILRYIA
RKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDFEKLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAY
DVLERNQVFEPSCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFTKMAVFGNK
>gi|999827|pdb|1HNG|B Chain B, Cd2 (Rat) >gi|999826|pdb|1HNG|A Chain A, Cd2 (Rat)
RDSGTVWGALGHGINLNIPNFQMTDDIDEVRWERGSTLVAEFKRKMKPFLKSGAFEILANGDLKIKNLTRDDSGTYNVTV
YSTNGTRILNKALDLRILEMVSKPMIYWECSNATLTCEVLEGTDVELKLYQGKEHLRSLRQKTMSYQWTNLRAPFKCKAV
NRVSQESEMEVVNCPE
>gi|515143|pdb|1HOC|A Chain A, Murine Class I Major Histocompatibility Complex Consisting Of H-2db, B2-Microglobulin, And A 9-Residue Peptide
GPHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWERETQKAKGQEQWFRVSLRN
LLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNEDLKTWTAADMAAQITRRKWEQSGAAEHYKAYL
EGECVEWLHRYLKNGNATLLRTDSPKAHVTHHPRSKGEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGT
FQKWASVVVPLGKEQNYTCRVYHEGLPEPLTL
>gi|443020|pdb|1HOM|  Antennapedia Protein (Homeodomain) (Nmr, 19 Structures)
MRKRGRQTYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKENKTKGEPG
>gi|1065308|pdb|1HPG|A Chain A, Glutamic Acid-Specific Protease (Glu-Sgp) (E.C.3.4.21.82) Complexed With A Tetrapeptide Ligand
VLGGGAIYGGGSRCSAAFNVTKGGARYFVTAGHCTNISANWSASSGGSVVGVREGTSFPTNDYGIVRYTDGSSPAGTVDL
YNGSTQDISSAANAVVGQAIKKSGSTTKVTSGTVTAVNVTVNYGDGPVYNMVRTTACSAGGDSGGAHFAGSVALGIHSGS
SGCSGTAGSAIHQPVTEALSAYGVTVY
>gi|576156|pdb|1HPL|B Chain B, Lipase (E.C.3.1.1.3) (Triacylglycerol Hydrolase) >gi|576155|pdb|1HPL|A Chain A, Lipase (E.C.3.1.1.3) (Triacylglycerol Hydrolase)
NEVCYERLGCFSDDSPWAGIVERPLKILPWSPEKVNTRFLLYTNENPDNFQEIVADPSTIQSSNFNTGRKTRFIIHGFID
KGEESWLSTMCQNMFKVESVNCICVDWKSGSRTAYSQASQNVRIVGAEVAYLVGVLQSSFDYSPSNVHIIGHSLGSHAAG
EAGRRTNGAVGRITGLDPAEPCFQGTPELVRLDPSDAQFVDVIHTDIAPFIPNLGFGMSQTAGHLDFFPNGGKEMPGCQK
NVLSQIVDIDGIWQGTRDFAACNHLRSYKYYTDSILNPDGFAGFSCASYSDFTANKCFPCSSEGCPQMGHYADRFPGRTK
GVGQLFYLNTGDASNFARWRYRVDVTLSGKKVTGHVLVSLFGNKGNSRQYEIFQGTLKPDNTYSNEFDSDVEVGDLEKVK
FIWYNNVINLTLPKVGASKITVERNDGSVFNFCSEETVREDVLLTLTAC
>gi|443023|pdb|1HPT|  Human Pancreatic Secretory Trypsin Inhibitor Variant 3 >gi|442733|pdb|1CGI|I Chain I, Alpha-Chymotrypsinogen Complex With Human Pancreatic Secretory Trypsin Inhibitor Variant 3
DSLGREAKCYNELNGCTYEYRPVCGTDGDTYPNECVLCFENRKRQTSILIQKSGPC
>gi|230009|pdb|1HR3|C Chain C, Hemerythrin (Azido,Met) >gi|230008|pdb|1HR3|B Chain B, Hemerythrin (Azido,Met) >gi|230007|pdb|1HR3|A Chain A, Hemerythrin (Azido,Met)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
>gi|494192|pdb|1HRA|  Retinoic Acid Receptor (Human) (Beta Dna-Binding Domain) (Nmr, 15 Structures)
MPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRN
>gi|230010|pdb|1HRB|  Hemerythrin B
GFPIPDPYVWDPSFRTFYSIIDDEHKTLFNGIFHLAIDDNADNLGELRRCTGKHFLNQEVLMEASQYQFYDEHKKEHDGF
INALDNWKGDVKWAKAWLVNHIKTIDFKYKGKI
>gi|640061|pdb|1HRF|  Heregulin-Alpha (Epidermal Growth Factor-Like Domain) (Nmr, 10 Structures) >gi|640060|pdb|1HRE|   Heregulin-Alpha (Epidermal Growth Factor-Like Domain) (Nmr, Minimized Average Structure)
GTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCQPGFTGARCTENVPMKVQNQEKAEELYQK
>gi|230012|pdb|1HRH|B Chain B, Ribonuclease H Domain Of HIV-1 Reverse Transcriptase >gi|230011|pdb|1HRH|A Chain A, Ribonuclease H Domain Of HIV-1 Reverse Transcriptase
YQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGII
QAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKILFL
>gi|999870|pdb|1HRM|  Myoglobin Mutant With His 93 Replaced By Tyr (H93y)
GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGTVVLTALGGILKKKG
HHEAELKPLAQSYATKHKIPIKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELGFQG
>gi|1065327|pdb|1HRN|B Chain B, Renin Complexed With Polyhydroxymonoamide Inhibitor Bila 980 >gi|1065326|pdb|1HRN|A Chain A, Renin Complexed With Polyhydroxymonoamide Inhibitor Bila 980 >gi|1310897|pdb|1BIM|B Chain B, Mol_id: 1; Molecule: Renin; Chain: A, B; Engineered: Yes; Heterogen: Butanediamide Inhibitor Bila 2151; Other_details: Glycosylated >gi|1310896|pdb|1BIM|A Chain A, Mol_id: 1; Molecule: Renin; Chain: A, B; Engineered: Yes; Heterogen: Butanediamide Inhibitor Bila 2151; Other_details: Glycosylated >gi|1310899|pdb|1BIL|B Chain B, Mol_id: 1; Molecule: Renin; Chain: A, B; Engineered: Yes; Heterogen: Butanediamide Inhibitor Bila 1908; Other_details: Glycosylated >gi|1310898|pdb|1BIL|A Chain A, Mol_id: 1; Molecule: Renin; Chain: A, B; Engineered: Yes; Heterogen: Butanediamide Inhibitor Bila 1908; Other_details: Glycosylated
GNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRY
STGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYN
RDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLM
EALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKF
YTEFDRRNNRIGFALAR
>gi|230018|pdb|1HSA|F Chain F, Human Class I Histocompatibility Antigen HLA-B(Asterisk)2705 >gi|230015|pdb|1HSA|C Chain C, Human Class I Histocompatibility Antigen HLA-B(Asterisk)2705
ARAAAAAAA
>gi|1421457|pdb|1HSN|  High Mobility Group Protein 1 (Hmg1) Box 2, Complexed With Mercaptoethanol (Nmr, 49 Structures) >gi|1421453|pdb|1HSM|   High Mobility Group Protein 1 (Hmg1) Box 2, Complexed With Mercaptoethanol (Nmr, Minimized Average Structure)
XAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAA
>gi|443033|pdb|1HST|B Chain B, Histone H5 (Globular Domain) >gi|443032|pdb|1HST|A Chain A, Histone H5 (Globular Domain)
SRRSASHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGVLKQTKGVGASGSFRLAKS
DKAKRSPGKK
>gi|1127130|pdb|1HTD|B Chain B, Mol_id: 1; Molecule: Atrolysin C; Chain: A, B; Synonym: Hemorrhagic Toxin C, Form D; Ec: 3.4.24.42 >gi|1127129|pdb|1HTD|A Chain A, Mol_id: 1; Molecule: Atrolysin C; Chain: A, B; Synonym: Hemorrhagic Toxin C, Form D; Ec: 3.4.24.42 >gi|1311407|pdb|1ATL|B Chain B, Mol_id: 1; Molecule: Atrolysin C; Chain: A, B, C, D; Synonym: Hemorrhagic Toxin C, Form D; Ec: 3.4.24.42; Heterogen: Sc 44463 >gi|1311405|pdb|1ATL|A Chain A, Mol_id: 1; Molecule: Atrolysin C; Chain: A, B, C, D; Synonym: Hemorrhagic Toxin C, Form D; Ec: 3.4.24.42; Heterogen: Sc 44463
QNLPQRYIELVVVADHRVFMKYNSDLNTIRTRVHEIVNFINGFYRSLNIHVSLTDLEIWSNEDQINIQSASSDTLNAFAE
WRETDLLNRKSHDNAQLLTAIELDEETLGLAPLGTMCDPKLSIGIVQDHSPINLLMGVTMAHELGHNLGMEHDGKDCLRG
ASLCIMRPGLTKGRSYEFSDDSMHYYERFLKQYKPQCILNKP
>gi|1065350|pdb|1HTL|A Chain A, Heat Labile Enterotoxin (Lt) Mutant With Val A 97 Replaced By Lys (V(A 97)k) (Synchrotron X-Ray Diffraction)
NGDRLYRADSRPPDEIKRSGGLMPRGHNEYFDRGTQMNINLYDHARGTQTGFVRYDDGYVSTSLSLRSAHLAGQSILSGY
STYYIYVIATAPNMFNKNDVLGVYSPHPYEQEVSALGGIPYSQIYGWYRVNFGVIDERLHRNREYRDRYYRNLNIAPAED
GYRLAGFPPDHQAWREEPWIHHAPQGCGNSS
>gi|999898|pdb|1HTM|E Chain E, Hemagglutinin Ectodomain (Soluble Fragment, Tbha2) >gi|999896|pdb|1HTM|C Chain C, Hemagglutinin Ectodomain (Soluble Fragment, Tbha2) >gi|999894|pdb|1HTM|A Chain A, Hemagglutinin Ectodomain (Soluble Fragment, Tbha2)
QDLPGNDNSTATLCLGHHAVPNGTLVK
>gi|999899|pdb|1HTM|F Chain F, Hemagglutinin Ectodomain (Soluble Fragment, Tbha2) >gi|999897|pdb|1HTM|D Chain D, Hemagglutinin Ectodomain (Soluble Fragment, Tbha2) >gi|999895|pdb|1HTM|B Chain B, Hemagglutinin Ectodomain (Soluble Fragment, Tbha2)
LKSTQAAIDQINGKLNRVIEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNK
LFEKTRRQLRENAEEMGNGCFKIYHKCDNACIESIRNGTYDHDVYRDEALNNRFQIKG
>gi|999901|pdb|1HTR|P Chain P, Progastricsin (Pepsinogen C) (E.C.3.4.23.3)
AVVKVPLKKFKSIRETMKEKGLLGEFLRTHKYDPAWKYRFGDL
>gi|1311009|pdb|1HUL|B Chain B, Mol_id: 1; Molecule: Interleukin-5; Chain: A, B; Engineered: Yes >gi|1311008|pdb|1HUL|A Chain A, Mol_id: 1; Molecule: Interleukin-5; Chain: A, B; Engineered: Yes
IPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQGIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKK
KCGEERRRVNQFLDYLQEFLGVMNTEWI
>gi|1311344|pdb|1HUP|  Alpha-Helical Coiled-Coil Mol_id: 1; Molecule: Mannose-Binding Protein; Chain: Null; Domain: Neck And Lectin Domain; Engineered: Yes
AASERKALQTEMARIKKWLTFSLGKQVGNKFFLTNGEIMTFEKVKALCVKFQASVATPRNAAENGAIQNLIKEEAFLGIT
DEKTEGQFVDLTGNRLTYTNWNEGEPNNAGSDEDCVLLLKNGQWNDVPCSTSHLAVCEFPI
>gi|494196|pdb|1HUW|  Human Growth Hormone Mutant With Phe 10 Replaced By Ala, Met 14 Replaced By Trp, His 18 Replaced By Asp, His 21 Replaced By Asn, Lys 41 Replaced By Ile, Tyr 42 Replaced By His, Leu 45 Replaced By Trp, Gln 46 Replaced By Trp, Phe 54 Replaced By Pro, Arg 64 Replaced By Lys, Arg 167 Replaced Asn, Asp 171 Replaced By Ser, Glu 174 Replaced By Ser, Phe 176 Replaced By Tyr, Ile 179 Replaced By Thr (F10a, M14w,H18d,H21n,K41i,Y42h,L45w,Q46w,F54p,R64k,R167n,D171s, E174s,F176y,I179t)
FPTIPLSRLADNAWLRADRLNQLAFDTYQEFEEAYIPKEQIHSFWWNPQTSLCPSESIPTPSNKEETQQKSNLELLRISL
LLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEALLKNYGLLYCFNKDMSKVSTYLRTVQCRSV
EGSCGF