4334 |
1DKR |
PDB NFT |
CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION. |
>1dkr_A mol:protein length:317 PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE
MSNQYGDKNLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQINIEESIRGCDCYIIQSTSDPVNEHIMELLIMVDALKRASAKTINIVIPYYGYARQDRKARSREPITAKLFANLLETAGATRVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLEDIVIVSPDHGGVTRARKLADRLKAPIAIIDKRRPRPNVAEVMNIVGNIEGKTAILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVLSGPAVERINNSTIKELVVTNSIKLPEEKKIERFKQLSVGPLLAEAIIRVHEQQSVSYLFS
>1dkr_B mol:protein length:317 PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE
MSNQYGDKNLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQINIEESIRGCDCYIIQSTSDPVNEHIMELLIMVDALKRASAKTINIVIPYYGYARQDRKARSREPITAKLFANLLETAGATRVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLEDIVIVSPDHGGVTRARKLADRLKAPIAIIDKRRPRPNVAEVMNIVGNIEGKTAILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVLSGPAVERINNSTIKELVVTNSIKLPEEKKIERFKQLSVGPLLAEAIIRVHEQQSVSYLFS |
4334 |
HLA04513 B*51:01:15 |
HLA NFT |
B*51:01:15 |
>HLA:HLA04513 B*51:01:15 181 bp SHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYWDRNTQIFKTNTQTYRENLRIALRYYNQSEAGSHTWQTMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQLRAYLEGLCVEWLRRHLENGKETLQRA |
4335 |
HLA04514 B*44:92 |
HLA NFT |
B*44:92 |
>HLA:HLA04514 B*44:92 181 bp SHSMRYFYTAMSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRENLRTALRYYNQSEAGSHIIQRMYGCDVGPDGRLLRGYDQDAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARMAEQLRAYLEGLCVESLRRYLENGKETLQRA |
4335 |
1DKS |
PDB NFT |
CKSHS1: HUMAN CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1 IN COMPLEX WITH PHOSPHATE |
>1dks_A mol:protein length:79 CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1
MSHKQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMIHEPEPHILLFRRPLPKKPKK
>1dks_B mol:protein length:79 CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1
MSHKQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMIHEPEPHILLFRRPLPKKPKK |
4335 |
A9N949 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|A9N949|ACCA_COXBR Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Coxiella burnetii (strain RSA 331 / Henzerling II) OX=360115 GN=accA PE=3 SV=1 MNLDYLDFEQPIAELQAKIDELRRVGTSQEINLTEEVNKLEEKNAQLTRQIFSNLTAQQIVQLARHPLRPYTLDYIQRIFTDFNELHGDRHYSQASAIIGGLARLNGEPVMVIGHQKGRTTQEKIYRNFGMARPEGFRKALRLMKLAERFSIPVITLIDTPGAYPGIGAEERNQSEAIARNLFEMAQLKIPIICTIIGEGCSGGALAIGVGDRTLMLQYAYYSVISPEGCASILWKSAEKAGEAAEALGLTANRLYELGLIDEIIKEPLGGAHRDTDAMAEKLKKHLQANLTNLQAKSANDLLEERYRRWLSYGKD |
4336 |
Q83BJ8 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|Q83BJ8|ACCA_COXBU Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Coxiella burnetii (strain RSA 493 / Nine Mile phase I) OX=227377 GN=accA PE=3 SV=1 MNLDYLDFEQPIAELQAKIDELRRVGTSQEINLTEEVNKLEEKNAQLTRQIFSNLTAQQIVQLARHPLRPYTLDYIQRIFTDFNELHGDRHYSQASAIIGGLARLNGEPVMVIGHQKGRTTQEKIYRNFGMARPEGFRKALRLMKLAERFSIPVITLIDTPGAYPGIGAEERNQSEAIARNLFEMAQLKIPIICTIIGEGCSGGALAIGVGDRTLMLQYAYYSVISPEGCASILWKSAEKAGEAAEALGLTANRLHELGLIDEIIKEPLGGAHRDTDAMAEKLKKHLQANLTNLQAKSANDLLEERYRRWLSYGKD |
4336 |
1DKT |
PDB NFT |
CKSHS1: HUMAN CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1 COMPLEX WITH METAVANADATE |
>1dkt_A mol:protein length:79 CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1
MSHKQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMIHEPEPHILLFRRPLPKKPKK
>1dkt_B mol:protein length:79 CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1
MSHKQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMIHEPEPHILLFRRPLPKKPKK |
4336 |
HLA04515 B*08:52 |
HLA NFT |
B*08:52 |
>HLA:HLA04515 B*08:52 181 bp SHSMRYFDTAMSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIFKTNTQTDRESLRIALRYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAARVAEQDRAYLEGTCVEWLRRYLENGKDTLERA |
4337 |
HLA04516 B*08:53:01 |
HLA NFT |
B*08:53:01 |
>HLA:HLA04516 B*08:53:01 181 bp SHSMRYFDTAMSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIFKTNTQTDRESLRNLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEQDRAYLEGTCVEWLRRYLENGKDTLERA |
4337 |
1DKU |
PDB NFT |
CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION. |
>1dku_A mol:protein length:317 PROTEIN (PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE)
MSNQYGDKNLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQINIEESIRGCDCYIIQSTSDPVNEHIMELLIMVDALKRASAKTINIVIPYYGYARQDRKARSREPITAKLFANLLETAGATRVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLEDIVIVSPDHGGVTRARKLADRLKAPIAIIDKRRPRPNVAEVMNIVGNIEGKTAILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVLSGPAVERINNSTIKELVVTNSIKLPEEKKIERFKQLSVGPLLAEAIIRVHEQQSVSYLFS
>1dku_B mol:protein length:317 PROTEIN (PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE)
MSNQYGDKNLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQINIEESIRGCDCYIIQSTSDPVNEHIMELLIMVDALKRASAKTINIVIPYYGYARQDRKARSREPITAKLFANLLETAGATRVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLEDIVIVSPDHGGVTRARKLADRLKAPIAIIDKRRPRPNVAEVMNIVGNIEGKTAILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVLSGPAVERINNSTIKELVVTNSIKLPEEKKIERFKQLSVGPLLAEAIIRVHEQQSVSYLFS |
4337 |
B1WPW6 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B1WPW6|ACCA_CROS5 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Crocosphaera subtropica (strain ATCC 51142 / BH68) OX=43989 GN=accA PE=3 SV=1 MSKNERRTFLLDFEKPLWELEARIEQIRHLAEENNVDVSEQIAQLESRAQNLRQEIFSSLTPSQRLQLARHPRRPSTLDYIQSIADEWFELHGDRGGYDDPALVGGVARLGGRPVVILGHQKGRDTKDNVARNFGMPAPGGYRKAIRLMEHANQFSMPILTFIDTPGAWAGVDAEKLGQGEAIAFNLRQMFSFDVPIICTVIGEGGSGGALGIGVGDKLMMLEHAVYTVATPEACAAILWKDAKKSSQAAVALKITAKDLKELGIIDTIIPEPSGAAHVNPLEAAAILKETLVNNLEELSNLTPEERKTLRYEKFRQIGVFLESDSNLALHS |
4338 |
A7MEM7 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|A7MEM7|ACCA_CROS8 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Cronobacter sakazakii (strain ATCC BAA-894) OX=290339 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMEMAERFNMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLKVPVICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSVIPEPLGGAHRNPEAMAQSLKTQLLADLADLDVLSKDDLLNRRYQRLMSYGYA |
4338 |
1DKW |
PDB NFT |
CRYSTAL STRUCTURE OF TRIOSE-PHOSPHATE ISOMERASE WITH MODIFIED SUBSTRATE BINDING SITE |
>1dkw_A mol:protein length:238 TRIOSEPHOSPHATE ISOMERASE
SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKFVIAAQNAGNEDSLPSLKDFGVNWIVLGHSERRWYYGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGLKPEFVDIIKATQ
>1dkw_B mol:protein length:238 TRIOSEPHOSPHATE ISOMERASE
SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKFVIAAQNAGNEDSLPSLKDFGVNWIVLGHSERRWYYGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGLKPEFVDIIKATQ |
4338 |
HLA04517 B*53:08:02 |
HLA NFT |
B*53:08:02 |
>HLA:HLA04517 B*53:08:02 181 bp SHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYWDRNTQIFKTNTQTYRENLRIALRYYNQSEAGSHIIQRMYGCDLGPDGRLLRGHDQSAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQLRAYLEGLCVEWLRRYLENGKETLQRA |
4339 |
HLA04518 B*51:24:03 |
HLA NFT |
B*51:24:03 |
>HLA:HLA04518 B*51:24:03 181 bp SHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYWDRNTQIFKTNTQTYRENLRIALRYYNQSEAGSHTWQTMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEQLRAYLEGLCVEWLRRHLENGKETLQRA |
4339 |
1DKX |
PDB NFT |
THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 1 SELENOMETHIONYL CRYSTALS |
>1dkx_A mol:protein length:219 SUBSTRATE BINDING DOMAIN OF DNAK
VLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFDELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHA
>1dkx_B mol:protein length:7 SUBSTRATE PEPTIDE (7 RESIDUES)
NRLLLTG |
4339 |
Q1LPF3 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|Q1LPF3|ACCA_CUPMC Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) OX=266264 GN=accA PE=3 SV=1 MKTTFLDFEQPIAELEAKIEELRFVQDDSAVDISEEISRLAGKSQQLTKDIYANLTPWQVAQIARHPQRPYTLDYVREIFTDFHELHGDRAFADDLSIVGGLARFNGQACMVIGHQKGRDTKERALRNFGMSKPEGYRKAKRLMELADKFGLPIFTFVDTPGAFPGIDAEERGQSEAIGHNLYVMAGLKVPLIATIIGEGGSGGALAIAVGDVVQMLQFATYAVISPEGCASILWKTAEKAPEAAEALGLTAHRLKALGLIDKIVSEPLGGAHRDAKGMATMLKRSLAESLRQFQGMSVKELQARRHERLMAYGKFKETGAQE |
4340 |
Q0KCA7 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|Q0KCA7|ACCA_CUPNH Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) OX=381666 GN=accA PE=3 SV=1 MKTTFLDFEQPIAELEAKIEELRFVQDDSAVDISEEISRLAGKSQQLTKDIYANLTPWQVAQIARHPQRPYTLDYVREIFTDFHELHGDRTFADDLSIIGGLARFNGQACMVIGHQKGRDTKERAMRNFGMPKPEGYRKAKRLMELADKFGLPIFTFVDTPGAFPGIDAEERGQSEAIGHNLYVMAGLKVPLIATIIGEGGSGGALAIAVGDVVQMLQFATYAVISPEGCASILWKTAEKAPEAAEALGLTAHRLKALGLIDKIVSEPLGGAHRDYKGMAAMLKRSLAESLRQFQGMSVKELQARRYERLLAYGKFKETGTQD |
4340 |
1DKY |
PDB NFT |
THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 2 NATIVE CRYSTALS |
>1dky_A mol:protein length:219 DNAK
VLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVSIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHA
>1dky_B mol:protein length:219 DNAK
VLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVSIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHA
>1dky_C mol:protein length:7 PEPTIDE SUBSTRATE
NRLLLTG
>1dky_D mol:protein length:7 PEPTIDE SUBSTRATE
NRLLLTG |
4340 |
HLA04519 B*44:93 |
HLA NFT |
B*44:93 |
>HLA:HLA04519 B*44:93 181 bp SHSMRYFYTAMSRPGRGEPRFITVGYVDDKLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRENLRTALRYYNQSEAGSHIIQRMYGCDVGPDGRLLRGYDQDAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQDRAYLEGLCVESLRRYLENGKETLQRA |
4341 |
HLA04520 B*08:54:01 |
HLA NFT |
B*08:54:01 |
>HLA:HLA04520 B*08:54:01 181 bp SHSMRYFDTAMSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRETQISKTNTQTYRESLRNLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAARVAEQDRAYLEGTCVEWLRRYLENGKDTLERA |
4341 |
1DKZ |
PDB NFT |
THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 1 NATIVE CRYSTALS |
>1dkz_A mol:protein length:219 SUBSTRATE BINDING DOMAIN OF DNAK
VLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVSIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHA
>1dkz_B mol:protein length:7 SUBSTRATE PEPTIDE (7 RESIDUES)
NRLLLTG |
4341 |
Q473D1 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|Q473D1|ACCA_CUPPJ Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) OX=264198 GN=accA PE=3 SV=1 MKTTFLDFEQPIAELEAKIEELRFVQDDSAVDISEEISRLAGKSQQLTKDIYANLTPWQVAQIARHPQRPYTLDYVREIFTDFHELHGDRTFADDLSIVGGLARFNGQSCMVIGHQKGRDTKERAMRNFGMPKPEGYRKAKRLMELADKFGLPIFTFVDTPGAFPGIDAEERGQSEAIGHNLYVMAGLKVPLIATIIGEGGSGGALAIAVGDVVQMLQFATYAVISPEGCASILWKTAEKAPEAAEALGLTAHRLKALGLIDKIVSEPLGGAHRDVKGMAAMLKRSLAESLRQFQGVSVKELQARRYERLLAYGKFKETGAQE |
4342 |
B3R4D3 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B3R4D3|ACCA_CUPTR Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1) OX=977880 GN=accA PE=3 SV=1 MKTTFLDFEQPIAELEAKIEELRFVQDDSAVDISEEISRLAGKSQQLTKDIYANLTPWQVAQIARHPQRPYTLDYVREIFTDFHELHGDRTFADDLSIIGGLARFNGQSCMVIGHQKGRDTKERAMRNFGMPKPEGYRKAKRLMELADKFGLPIFTFVDTPGAFPGIDAEERGQSEAIGHNLYVMAGLRVPLIATIIGEGGSGGALAIAVGDVVQMLQFATYAVISPEGCASILWKTAEKAPEAAEALGLTAHRLKALGLIDKIVSEPLGGAHRDYKGMAALLKRSLAESLRQFQGMSVKELQARRYERLLAYGKFKETGAQD |
4342 |
1DL0 |
PDB NFT |
SOLUTION STRUCTURE OF THE INSECTICIDAL NEUROTOXIN J-ATRACOTOXIN-HV1C |
>1dl0_A mol:protein length:37 J-ATRACOTOXIN-HV1C
AICTGADRPCAACCPCCPGTSCKAESNGVSYCRKDEP |
4342 |
HLA04521 B*35:01:18 |
HLA NFT |
B*35:01:18 |
>HLA:HLA04521 B*35:01:18 181 bp SHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYWDRNTQIFKTNTQTYRESLRNLRGYYNQSEAGSHIIQRMYGCDLGPDGRLLRGHDQSAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGLCVEWLRRYLENGKETLQRA |
4343 |
HLA04522 A*30:32 |
HLA NFT |
A*30:32 |
>HLA:HLA04522 A*30:32 181 bp SHSMRYFSTSVSRPGSGEPRFIAVGYVDDTQFVRFDSDAASQRMERRAPWIEQERPEYWDQETRNVKAHSQTDRENLGTLRGYYNQSEAGSHTIQIMYGCDVGSDGRFLRGYEQHAYDGKDYIALNEDLRSWTAADMAAQITQRKWEAARRAEQLRAYLEGTCVEWLRRYLENGKETLQRT |
4343 |
1DL2 |
PDB NFT |
CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION |
>1dl2_A mol:protein length:511 CLASS I ALPHA-1,2-MANNOSIDASE
GAGEMRDRIESMFLESWRDYSKHGWGYDVYGPIEHTSHNMPRGNQPLGWIIVDSVDTLMLMYNSSTLYKSEFEAEIQRSEHWINDVLDFDIDAEVNVFETTIRMLGGLLSAYHLSDVLEVGNKTVYLNKAIDLGDRLALAFLSTQTGIPYSSINLHSGQAVKNHADGGASSTAEFTTLQMEFKYLAYLTGNRTYWELVERVYEPLYKNNDLLNTYDGLVPIYTFPDTGKFGASTIRFGSRGDSFYEYLLKQYLLTHETLYYDLYRKSMEGMKKHLLAQSKPSSLWYIGEREQGLHGQLSPKMDHLVCFMGGLLASGSTEGLSIHEARRRPFFSKSDWDLAKGITDTCYQMYKQSSSGLAPEIVVFNDGNIKQDGWWRSSVGDFFVKPLDRHNLQRPETVESIMFMYHLSHDHKYREWGAEIATSFFENTCVDCNDPKLRRFTSLSDCITLPTKKSNNMESFWLAETLKYLYILFLDEFDLTKVVFNTEAHPFPVLDEEILKSQSLTTGWSL |
4343 |
O19903 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|O19903|ACCA_CYACA Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Cyanidium caldarium OX=2771 GN=accA PE=3 SV=1 MKMLDKTLPLEELESSLTKTESKAYYLSKLVYRHDKVVNNKAHILQRKLLNLKKQLFYGLTSYQKLCVARHKRRPTTLDYIEYLLDSWIELHGDRRGSDDPAIITGIGRIGRRSVVVLGQQKGRNTKENVLRNFGMSSPGGYRKALRVMEHANKFKLPILTFIDTPGALAGVSAEKSGQAEAIATNLKKMFSFEVPIISTIIGEGGSGGALGICIGNYVMMFENSIYTVATPEACSSILWKDSTKAADAAEALKVRAEDLLTLKIIDEIIPEPFGVAHDYPLLMVRILKNKIRDQLDFFDTFSPSELKHHRYLKFRKLGLYYDC |
4344 |
Q85G50 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|Q85G50|ACCA_CYAM1 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Cyanidioschyzon merolae (strain 10D) OX=280699 GN=accA PE=3 SV=1 METHFHEWQKSLQLIQQKSEELQREQIQLKSFERELRIINKWFYYGLHYEQKLQLARHPKRPTSLDYIEGMSQDWIELHGDRKGSDDQALITGIAQVEDETIVFLAHQKGRNTKENLQRNFGMPSPGGYRKALRIMNHANKFGLPLVTLIDTPGAWAGVEAEKEGQAHAIATCLQTMFSLEVPMISVIIGEGGSGGALAIGVSNWMMMLEHAVYTVATPEACAAILWKDASKSAEAAEALKIGAEDLLALGVIDEIIPEPIGCAHQDAASMTKRLKQKILRRLKQLKILSGKQLRAHRAERFRHLGYYVE |
4344 |
1DL3 |
PDB NFT |
CRYSTAL STRUCTURE OF MUTUALLY GENERATED MONOMERS OF DIMERIC PHOSPHORIBOSYLANTRANILATE ISOMERASE FROM THERMOTOGA MARITIMA |
>1dl3_A mol:protein length:203 PROTEIN (PHOSPHORIBOSYLANTRANILATE ISOMERASE)
MVRVKICGITNLEDALFSVESGADYVGFVFYPKSKRYISPEDARRISVELPVERVGVFVNEEPEKILDVASYVQLNAVQLHGEEPIELCRKIAERILVWKAVGVSNERDMERALNYREFPILLDTKTPEYGGSGKTFDWSLILPYRDRFRYLVLSGGLNPENVRSAIDVVRPFAVDVSSGVEAFPGKKDHDSIKMFIKNAKGL
>1dl3_B mol:protein length:203 PROTEIN (PHOSPHORIBOSYLANTRANILATE ISOMERASE)
MVRVKICGITNLEDALFSVESGADYVGFVFYPKSKRYISPEDARRISVELPVERVGVFVNEEPEKILDVASYVQLNAVQLHGEEPIELCRKIAERILVWKAVGVSNERDMERALNYREFPILLDTKTPEYGGSGKTFDWSLILPYRDRFRYLVLSGGLNPENVRSAIDVVRPFAVDVSSGVEAFPGKKDHDSIKMFIKNAKGL |
4344 |
HLA04523 A*26:42 |
HLA NFT |
A*26:42 |
>HLA:HLA04523 A*26:42 365 bp MAVMAPRTLVLLLSGALALTQTWAGSHSMRYFYTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRIWPRAPWIEQEGPEYWDRNTRNVKAHSQTDRANLGTLRGYYNQSEDGSHTIQRMYGCDVGPDGRFLRGYQQDAYDGKDYIALNEDLRSWTAADMAAQITQRKWETAHEAEQWRAYLEGRCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWASVVVPSGQEQRYTCHVQHEGLPKPLTLRWEPSSQPTIPIVGIIAGLVLFGAVIAGAVVAAVMWRRKSSDRKGGSYSQAASSDSAQGSDMSLTACKV |
4345 |
HLA04524 A*01:01:12 |
HLA NFT |
A*01:01:12 |
>HLA:HLA04524 A*01:01:12 181 bp SHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLGTLRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVYLEGRCVDGLRRYLENGKETLQRT |
4345 |
1DL4 |
PDB NFT |
THE SOLUTION STRUCTURE OF A BAY-REGION 1S-BENZ[A]ANTHRACENE OXIDE ADDUCT AT THE N6 POSITION OF ADENINE OF AN OLIGODEOXYNUCLEOTIDE CONTAINING THE HUMAN N-RAS CODON 61 SEQUENCE |
>1dl4_A mol:na length:11 DNA (5'-D(*CP*GP*GP*AP*CP*(BZA)AP*AP*GP*AP*AP*G)-3')
CGGACAAGAAG
>1dl4_B mol:na length:11 DNA (5'-D(*CP*TP*TP*CP*TP*TP*GP*TP*CP*CP*G)-3')
CTTCTTGTCCG |
4345 |
B8HSZ5 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B8HSZ5|ACCA_CYAP4 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Cyanothece sp. (strain PCC 7425 / ATCC 29141) OX=395961 GN=accA PE=3 SV=1 MATERKPILLEFEKPLAELEAQINQVRQKSAELGVDVSDQIRELENNSTQLRQEIFSKLTPSQKLQLARHPRRPSTLDYIQAISDEWMELHGDRYGSDDPAIVAGVARLAGQPVVMLGQQKGRDTKDNVARNFGMASPSGYRKAIRIMEHADRFGMPILTFIDTPAAWAGIEAEQYGQGEAIAYNLREMFRLEVPIICTVIGEGGSGGALGIGVGDRLLMFEHAIYSVAPPEACAAILWRDAQKAPLAAEALKITAADLQKLGLIDEILPEPLGGAHVDPVGATEILKTSLIAHLRQLSQMSSPQRRELRYQKFRRMGIFTQSAA |
4346 |
Q47HT1 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|Q47HT1|ACCA_DECAR Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Dechloromonas aromatica (strain RCB) OX=159087 GN=accA PE=3 SV=2 MKTSFLDFEQSIADLEAKIEELRFVQDDSAVDISEEIGRLEKKSGQLTKDIYAKLTPWQISQVARHPQRPYTLDYLSLIFTDFEELHGDRAFADDHAIVGGLARFNGQPVMVIGHQKGRDTKEKIYRNFGMPRPEGYRKALRLMKLAEKFGIPVMTFVDTPGAYPGIDAEERGQSEAIGRNLYVMAELKVPVIVTIIGEGGSGGALAIAVGDTLQMLQYSTYSVISPEGCASILWKSSERAPEAAETMGITAQRLKTLGLVDKIVNEPLGGAHRDHAAMAQNLKKALQDALKQLSGLSTAELLATRYERLMSYGRFKEQAVS |
4346 |
1DL5 |
PDB NFT |
PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE |
>1dl5_A mol:protein length:317 PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE
MREKLFWILKKYGVSDHIAKAFLEIPREEFLTKSYPLSYVYEDIVLVSYDDGEEYSTSSQPSLMALFMEWVGLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVERLGIENVIFVCGDGYYGVPEFSPYDVIFVTVGVDEVPETWFTQLKEGGRVIVPINLKLSRRQPAFLFKKKDPYLVGNYKLETRFITAGGNLGNLLERNRKLLREFPFNREILLVRSHIFVELVDLLTRRLTEIDGTFYYAGPNGVVEFLDDRMRIYGDAPEIENLLTQWESCGYRSFEYLMLHVGYNAFSHISCSI
>1dl5_B mol:protein length:317 PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE
MREKLFWILKKYGVSDHIAKAFLEIPREEFLTKSYPLSYVYEDIVLVSYDDGEEYSTSSQPSLMALFMEWVGLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVERLGIENVIFVCGDGYYGVPEFSPYDVIFVTVGVDEVPETWFTQLKEGGRVIVPINLKLSRRQPAFLFKKKDPYLVGNYKLETRFITAGGNLGNLLERNRKLLREFPFNREILLVRSHIFVELVDLLTRRLTEIDGTFYYAGPNGVVEFLDDRMRIYGDAPEIENLLTQWESCGYRSFEYLMLHVGYNAFSHISCSI |
4346 |
HLA04525 A*01:49 |
HLA NFT |
A*01:49 |
>HLA:HLA04525 A*01:49 181 bp SHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLGTLRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVYLESRCVDGLRRYLENGKETLQRT |
4347 |
HLA04526 B*44:94 |
HLA NFT |
B*44:94 |
>HLA:HLA04526 B*44:94 181 bp SHSMRYFYTAMSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRENLRTALRYYNQSEAGSHIIQRMYGCDVGPDGRLLRGYDQDAYDGKDYIALNEDLSSWTAADTAAQITHRKWEAARVAEQLRAYLEGLCVESLRRYLENGKETLQRA |
4347 |
1DL6 |
PDB NFT |
SOLUTION STRUCTURE OF HUMAN TFIIB N-TERMINAL DOMAIN |
>1dl6_A mol:protein length:58 TRANSCRIPTION FACTOR II B (TFIIB)
ASTSRLDALPRVTCPNHPDAILVEDYRAGDMICPECGLVVGDRVIDVGSEWRTFSNDK |
4347 |
Q9RV16 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|Q9RV16|ACCA_DEIRA Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) OX=243230 GN=accA PE=3 SV=1 MTSTPADALRELEARVRDLEATAERTGQNLDAALAPLRTQLETLRREHAAGLSRWDRVQLARTPGRPTALDYVDRLCSDWTELHGDRRFGDDPALIGGPARWQGRPVMLLLQQKGRDTKTKIKRRFGSANPEGYRKAIRLMDLADRFGLPVVSLIDTQGAYPGLEAEERGQGWAIAESIQRMVRLRVPAVCAVIGEGGSGGALAIGVGNRVLIQENAWYSVISPEGAASILWRDAAQAPLAAEALRVTAADLLDMGIVEEVVPEPPGGAHLDMDAAAEALGSVISRHLDDLSALTPDDLLAQRAARFRSLGAFEER |
4348 |
B8FTK8 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B8FTK8|ACCA_DESHD Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Desulfitobacterium hafniense (strain DSM 10664 / DCB-2) OX=272564 GN=accA PE=3 SV=1 MAQHFDFEKPILELEQKIAELQEFSKEKDINLSPEISKLMRRLVRLRKEIYGNLEPWQKVQIARHMERPNFYDYAPLLFEDFMEFKGDRLFADDKAIVGGIAIFQGIPVTVVSHIKGRGTKENIQRNFGMPHPEGYRKALRLMDQAEKFHRPILTFIDTPGAACDLEAEERGQGEAIARCLQAMAGYSVPIICTVIGEGGSGGALALGVGNKVLLLENSFYSVIAPESCASILWKDPGKAKEAASALKFTAQDLLELGIADGIIKEPLGGAHRSVERTAEEMKKTIAEALAELRELPPDELRTMRYEKLMNYGEFEEKA |
4348 |
1DL7 |
PDB NFT |
THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINE |
>1dl7_L mol:protein length:109 PROTEIN (ANTIBODY M3C65 (LIGHT CHAIN))
QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTKHRTPGAPARFSGSLIGDKAALTITGAQTEDEAIYFCALWYSNHWVFGGGTKLTVL
>1dl7_H mol:protein length:112 PROTEIN (ANTIBODY M3C65 (HEAVY CHAIN))
QVQLKESGPGLVAPSQSLSITCTVSGFSLTGYGVNWVRQPPGKGLEWLGMIWGDGSTDYNSALKSRLNISKDKSKSQVFLRMYSLQTDDTARYYCARDYGPYWGQGTLVTVS |
4348 |
HLA04527 A*01:50 |
HLA NFT |
A*01:50 |
>HLA:HLA04527 A*01:50 181 bp SHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLGTLRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQEAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVYLEGRCVDGLRRYLENGKETLQRT |
4349 |
HLA04528 A*03:65 |
HLA NFT |
A*03:65 |
>HLA:HLA04528 A*03:65 181 bp SHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDQETRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQIMYGCDVGSDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAAHEAEQQRAYLDGTCVEWLRRYLENGKETLQRT |
4349 |
1DL8 |
PDB NFT |
CRYSTAL STRUCTURE OF 5-F-9-AMINO-(N-(2-DIMETHYLAMINO)ETHYL)ACRIDINE-4-CARBOXAMIDE BOUND TO D(CGTACG)2 |
>1dl8_A mol:na length:6 DNA (5'-D(*CP*GP*TP*AP*CP*G)-3')
CGTACG |
4349 |
Q24XY7 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|Q24XY7|ACCA_DESHY Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Desulfitobacterium hafniense (strain Y51) OX=138119 GN=accA PE=3 SV=1 MAQHFDFEKPILELEQKIAELQEFSKEKDINLSPEISKLMRRLVRLRKEIYGNLEPWQKVQIARHMERPNFYDYAPLLFEDFMEFKGDRLFADDKAIVGGIAIFQGIPVTVVSHIKGRGTKENIQRNFGMPHPEGYRKALRLMDQAEKFHRPILTFIDTPGAACDLEAEERGQGEAIARCLQAMAGYSVPIICTVIGEGGSGGALALGVGNKVLLLENSFYSVIAPESCASILWKDPGKAKEAASALKFTAQDLLELGIADGIIKEPLGGAHRSVERTAEEMKKTIAEALAELRELPPDELRTMRYEKLMNYGEFEEKA |
4350 |
A5EXQ5 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|A5EXQ5|ACCA_DICNV Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Dichelobacter nodosus (strain VCS1703A) OX=246195 GN=accA PE=3 SV=1 MNPEYLDFEQPIAELEYKLNELKQFSEQSKVDISDEVERLKTKLERLTGDIYSDLSDWQIAQVARHPKRPYTLDYIPHIFTDFRELHGDRHYADDMAIVGGLARLGQRSVMVIGHEKGRDTKAKVSRNFGMPRPEGYRKALRLMKLAEKFKIPVITFIDTPGAYPGVGAEKRGQSEAIARNLYEMAVLNTPIIACVIGEGGSGGALALGVADTVMMLQYGMYSVISPEGCASILWRDAAMAEEAVTILQVTSTRLKKLNLIDTIITEPSGGAHRDVAEMSRTLHDAFLSELDRLEAMDDATRIHQRLQKLRAYGNFLGE |
4350 |
1DLA |
PDB NFT |
NOVEL NADPH-BINDING DOMAIN REVEALED BY THE CRYSTAL STRUCTURE OF ALDOSE REDUCTASE |
>1dla_A mol:protein length:314 ALDOSE REDUCTASE
SHLVLYTGAKMPILGLGTWKSPPGKVTEAVKVAIDLGYRHIDCAHVYQNENEVGLGLQEKLQGQVVKREDLFIVSKLWCTDHEKNLVKGACQTTLRDLKLDYLDLYLIHWPTGFKPGKDPFPLDGDGNVVPDESDFVETWEAMEELVDEGLVKAIGVSNFNHLQVEKILNKPGLKYKPAVNQIEVHPYLTQEKLIEYCKSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKYNKTTAQVLIRFPMQRNLIVIPKSVTPERIAENFQVFDFELSPEDMNTLLSYNRNWRVCALMSCASHKDYPFHEEY
>1dla_B mol:protein length:314 ALDOSE REDUCTASE
SHLVLYTGAKMPILGLGTWKSPPGKVTEAVKVAIDLGYRHIDCAHVYQNENEVGLGLQEKLQGQVVKREDLFIVSKLWCTDHEKNLVKGACQTTLRDLKLDYLDLYLIHWPTGFKPGKDPFPLDGDGNVVPDESDFVETWEAMEELVDEGLVKAIGVSNFNHLQVEKILNKPGLKYKPAVNQIEVHPYLTQEKLIEYCKSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKYNKTTAQVLIRFPMQRNLIVIPKSVTPERIAENFQVFDFELSPEDMNTLLSYNRNWRVCALMSCASHKDYPFHEEY
>1dla_C mol:protein length:314 ALDOSE REDUCTASE
SHLVLYTGAKMPILGLGTWKSPPGKVTEAVKVAIDLGYRHIDCAHVYQNENEVGLGLQEKLQGQVVKREDLFIVSKLWCTDHEKNLVKGACQTTLRDLKLDYLDLYLIHWPTGFKPGKDPFPLDGDGNVVPDESDFVETWEAMEELVDEGLVKAIGVSNFNHLQVEKILNKPGLKYKPAVNQIEVHPYLTQEKLIEYCKSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKYNKTTAQVLIRFPMQRNLIVIPKSVTPERIAENFQVFDFELSPEDMNTLLSYNRNWRVCALMSCASHKDYPFHEEY
>1dla_D mol:protein length:314 ALDOSE REDUCTASE
SHLVLYTGAKMPILGLGTWKSPPGKVTEAVKVAIDLGYRHIDCAHVYQNENEVGLGLQEKLQGQVVKREDLFIVSKLWCTDHEKNLVKGACQTTLRDLKLDYLDLYLIHWPTGFKPGKDPFPLDGDGNVVPDESDFVETWEAMEELVDEGLVKAIGVSNFNHLQVEKILNKPGLKYKPAVNQIEVHPYLTQEKLIEYCKSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKYNKTTAQVLIRFPMQRNLIVIPKSVTPERIAENFQVFDFELSPEDMNTLLSYNRNWRVCALMSCASHKDYPFHEEY |
4350 |
HLA04529 A*11:01:16 |
HLA NFT |
A*11:01:16 |
>HLA:HLA04529 A*11:01:16 181 bp SHSMRYFYTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDQETRNVKAQSQTDRVDLGTLRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAAHAAEQQRAYLEGRCVEWLRRYLENGKETLQRT |
4351 |
HLA04530 A*03:66 |
HLA NFT |
A*03:66 |
>HLA:HLA04530 A*03:66 181 bp SHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDQETRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQIMYGCDVGSDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAAHEAEQRRAYLDGTCVEWLRRYLENGKETLQRT |
4351 |
1DLB |
PDB NFT |
HELICAL INTERACTIONS IN THE HIV-1 GP41 CORE REVEALS STRUCTURAL BASIS FOR THE INHIBITORY ACTIVITY OF GP41 PEPTIDES |
>1dlb_A mol:protein length:68 HIV-1 ENVELOPE GLYCOPROTEIN GP41
SGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARSGGRGGWMEWDREINNYTSLIHSLIEESQNLQEK |
4351 |
A7ZHS5 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|A7ZHS5|ACCA_ECO24 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O139:H28 (strain E24377A / ETEC) OX=331111 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4352 |
B7UJ86 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B7UJ86|ACCA_ECO27 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O127:H6 (strain E2348/69 / EPEC) OX=574521 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLSVPTICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4352 |
1DLC |
PDB NFT |
CRYSTAL STRUCTURE OF INSECTICIDAL DELTA-ENDOTOXIN FROM BACILLUS THURINGIENSIS AT 2.5 ANGSTROMS RESOLUTION |
>1dlc_A mol:protein length:584 DELTA-ENDOTOXIN CRYIIIA
TTKDVIQKGISVVGDLLGVVGFPFGGALVSFYTNFLNTIWPSEDPWKAFMEQVEALMDQKIADYAKNKALAELQGLQNNVEDYVSALSSWQKNPVSSRNPHSQGRIRELFSQAESHFRNSMPSFAISGYEVLFLTTYAQAANTHLFLLKDAQIYGEEWGYEKEDIAEFYKRQLKLTQEYTDHCVKWYNVGLDKLRGSSYESWVNFNRYRREMTLTVLDLIALFPLYDVRLYPKEVKTELTRDVLTDPIVGVNNLRGYGTTFSNIENYIRKPHLFDYLHRIQFHTRFQPGYYGNDSFNYWSGNYVSTRPSIGSNDIITSPFYGNKSSEPVQNLEFNGEKVYRAVANTNLAVWPSAVYSGVTKVEFSQYNDQTDEASTQTYDSKRNVGAVSWDSIDQLPPETTDEPLEKGYSHQLNYVMCFLMQGSRGTIPVLTWTHKSVDFFNMIDSKKITQLPLVKAYKLQSGASVVAGPRFTGGDIIQCTENGSAATIYVTPDVSYSQKYRARIHYASTSQITFTLSLDGAPFNQYYFDKTINKGDTLTYNSFNLASFSTPFELSGNNLQIGVTGLSAGDKVYIDKIEFIPVN |
4352 |
HLA04531 A*66:12 |
HLA NFT |
A*66:12 |
>HLA:HLA04531 A*66:12 181 bp SHSMRYFYTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDRNTRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQRMYGCDVGPDGRFLRGYQQDAYDGKDYIALNEDLRSWTAADMAAQITQRKWETAHEAEQWRAYLEGRCVEWLRRYLENGKETLQRT |
4353 |
HLA04532 B*14:17 |
HLA NFT |
B*14:17 |
>HLA:HLA04532 B*14:17 181 bp SHSMRYFYTAVSQPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQICKTNTQTDRESLRNLRGYYNQSEAGSHTLQWMYGCDVGPDGRLLRGYNQFAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQLRAYLEGTCVEWLRRHLENGKETLQRA |
4353 |
1DLE |
PDB NFT |
FACTOR B SERINE PROTEASE DOMAIN |
>1dle_A mol:protein length:298 COMPLEMENT FACTOR B
ADPDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL
>1dle_B mol:protein length:298 COMPLEMENT FACTOR B
ADPDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL |
4353 |
B7MBG6 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B7MBG6|ACCA_ECO45 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O45:K1 (strain S88 / ExPEC) OX=585035 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLTDLADLDVLSTEDLKNRRYQRLMSYGYA |
4354 |
B7LGP7 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B7LGP7|ACCA_ECO55 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli (strain 55989 / EAEC) OX=585055 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4354 |
1DLF |
PDB NFT |
HIGH RESOLUTION CRYSTAL STRUCTURE OF THE FV FRAGMENT FROM AN ANTI-DANSYL SWITCH VARIANT ANTIBODY IGG2A(S) CRYSTALLIZED AT PH 5.25 |
>1dlf_L mol:protein length:113 ANTI-DANSYL IMMUNOGLOBULIN IGG2A(S)
DVVMTQTPLSLPVSLGNQASISCRSSQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPFTFGSGTKLEIKR
>1dlf_H mol:protein length:124 ANTI-DANSYL IMMUNOGLOBULIN IGG2A(S)
EVKLEESGGGLVQPGGSMKLSCATSGFTFSDAWMDWVRQSPEKGLEWVAEIRNKANNHATYYAESVKGRFTISRDDSKRRVYLQMNTLRAEDTGIYYCTGIYYHYPWFAYWGQGTLVTVSAEPR |
4354 |
HLA04533 B*15:184 |
HLA NFT |
B*15:184 |
>HLA:HLA04533 B*15:184 181 bp SHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRMAPRAPWIEQEGPEYWDRETQISKTNTQTYRESLRNLRGYYNQSEAGSHTLQRTYGCDVGPDGRLLRGHDQSAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQWRAYLEGLCVEWLRRYLENGKETLQRA |
4355 |
HLA04534 B*44:02:11 |
HLA NFT |
B*44:02:11 |
>HLA:HLA04534 B*44:02:11 181 bp SHSMRYFYTAMSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRENLRTALRYYNQSEAGSHIIQRMYGCDVGPDGRLLRGYDQDAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQDRAYLEGLCVESLRRYLENGKETLQRA |
4355 |
1DLG |
PDB NFT |
CRYSTAL STRUCTURE OF THE C115S ENTEROBACTER CLOACAE MURA IN THE UN-LIGANDED STATE |
>1dlg_A mol:protein length:419 UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE MURA
MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVERDGSVWIDASNVNNFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGSAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTDMQAQFTLLNLVAEGTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIERVKGE
>1dlg_B mol:protein length:419 UDP-N-ACETYLGLUCOSAMINE ENOLPYRUVYL TRANSFERASE MURA
MDKFRVQGPTRLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDIDTTMKLLTQLGTKVERDGSVWIDASNVNNFSAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGSAIGARPVDLHIFGLEKLGAEIKLEEGYVKASVNGRLKGAHIVMDKVSVGATVTIMSAATLAEGTTIIENAAREPEIVDTANFLVALGAKISGQGTDRITIEGVERLGGGVYRVLPDRIETGTFLVAAAISGGKIVCRNAQPDTLDAVLAKLREAGADIETGEDWISLDMHGKRPKAVTVRTAPHPAFPTDMQAQFTLLNLVAEGTGVITETIFENRFMHVPELIRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIERVKGE |
4355 |
P0ABD6 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|P0ABD6|ACCA_ECO57 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O157:H7 OX=83334 GN=accA PE=3 SV=2 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4356 |
B5Z0G4 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B5Z0G4|ACCA_ECO5E Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O157:H7 (strain EC4115 / EHEC) OX=444450 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4356 |
1DLH |
PDB NFT |
CRYSTAL STRUCTURE OF THE HUMAN CLASS II MHC PROTEIN HLA-DR1 COMPLEXED WITH AN INFLUENZA VIRUS PEPTIDE |
>1dlh_A mol:protein length:180 CLASS II HISTOCOMPATIBILITY ANTIGEN (HLA-DR1) (ALPHA CHAIN)
EEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEFDA
>1dlh_D mol:protein length:180 CLASS II HISTOCOMPATIBILITY ANTIGEN (HLA-DR1) (ALPHA CHAIN)
EEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGALANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVTWLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEFDA
>1dlh_B mol:protein length:188 CLASS II HISTOCOMPATIBILITY ANTIGEN (HLA-DR1) (BETA CHAIN)
TRPRFLWQLKFECHFFNGTERVRLLERCIYNQEESVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQRRAAVDTYCRHNYGVGESFTVQRRVEPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRA
>1dlh_E mol:protein length:188 CLASS II HISTOCOMPATIBILITY ANTIGEN (HLA-DR1) (BETA CHAIN)
TRPRFLWQLKFECHFFNGTERVRLLERCIYNQEESVRFDSDVGEYRAVTELGRPDAEYWNSQKDLLEQRRAAVDTYCRHNYGVGESFTVQRRVEPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRA
>1dlh_C mol:protein length:13 ENTEROTOXIN TYPE B PRECURSOR
PKYVKQNTLKLAT
>1dlh_F mol:protein length:13 ENTEROTOXIN TYPE B PRECURSOR
PKYVKQNTLKLAT |
4356 |
HLA04535 B*49:08 |
HLA NFT |
B*49:08 |
>HLA:HLA04535 B*49:08 181 bp SHSMRYFHTAMSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRENLRIALRYYNQSEAGSHTWQRMYGCDLGPDGRLLRGYNQLAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQLRAYLEGLCLEWLRRYLENGKETLQRA |
4357 |
HLA04536 B*44:95 |
HLA NFT |
B*44:95 |
>HLA:HLA04536 B*44:95 181 bp SHSMRYFYTAMSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRENLRIALRYYNQSEAGSHIIQRMYGCDVGPDGRLLRGYDQDAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQDRAYLEGLCVESLRRYLENGKETLQRA |
4357 |
1DLI |
PDB NFT |
THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION |
>1dli_A mol:protein length:402 UDP-GLUCOSE DEHYDROGENASE
MKIAVAGSGYVGLSLGVLLSLQNEVTIVDILPSKVDKINNGLSPIQDEYIEYYLKSKQLSIKATLDSKAAYKEAELVIIATPTNYNSRINYFDTQHVETVIKEVLSVNSHATLIIKSTIPIGFITEMRQKFQTDRIIFSPEFLRESKALYDNLYPSRIIVSCEENDSPKVKADAEKFALLLKSAAKKNNVPVLIMGASEAEAVKLFANTYLALRVAYFNELDTYAESRKLNSHMIIQGISYDDRIGMHYNNPSFGYGGYCLPKDTKQLLANYNNIPQTLIEAIVSSNNVRKSYIAKQIINVLKEQESPVKVVGVYRLIMKSNSDNFRESAIKDVIDILKSKDIKIIIYEPMLNKLESEDQSVLVNDLENFKKQANIIVTNRYDNELQDVKNKVYSRDIFGRD |
4357 |
B7NIE7 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B7NIE7|ACCA_ECO7I Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O7:K1 (strain IAI39 / ExPEC) OX=585057 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLSVPTICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4358 |
B7MP45 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B7MP45|ACCA_ECO81 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O81 (strain ED1a) OX=585397 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4358 |
1DLJ |
PDB NFT |
THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION |
>1dlj_A mol:protein length:402 UDP-GLUCOSE DEHYDROGENASE
MKIAVAGSGYVGLSLGVLLSLQNEVTIVDILPSKVDKINNGLSPIQDEYIEYYLKSKQLSIKATLDSKAAYKEAELVIIATPTNYNSRINYFDTQHVETVIKEVLSVNSHATLIIKSTIPIGFITEMRQKFQTDRIIFSPEFLRESKALYDNLYPSRIIVSCEENDSPKVKADAEKFALLLKSAAKKNNVPVLIMGASEAEAVKLFANTYLALRVAYFNELDTYAESRKLNSHMIIQGISYDDRIGMHYNNPSFGYGGYSLPKDTKQLLANYNNIPQTLIEAIVSSNNVRKSYIAKQIINVLKEQESPVKVVGVYRLIMKSNSDNFRESAIKDVIDILKSKDIKIIIYEPMLNKLESEDQSVLVNDLENFKKQANIIVTNRYDNELQDVKNKVYSRDIFGRD |
4358 |
HLA04537 B*51:88 |
HLA NFT |
B*51:88 |
>HLA:HLA04537 B*51:88 181 bp SHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYWDRNTQIFKTNTQTYRENLRIALRYYNQSEAGSHTWQTMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQLRAYLDGLCVEWLRRHLENGKETLQRA |
4359 |
HLA04538 B*49:09 |
HLA NFT |
B*49:09 |
>HLA:HLA04538 B*49:09 181 bp SHSMRYFHTAMSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRENLRIALRYYNQSEAGSHTWQRMYGCDLGPDGRLLRGYNQLAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQLRAYLEGLCVEWLRRHLENGKETLQRA |
4359 |
1DLK |
PDB NFT |
CRYSTAL STRUCTURE ANALYSIS OF DELTA-CHYMOTRYPSIN BOUND TO A PEPTIDYL CHLOROMETHYL KETONE INHIBITOR |
>1dlk_A mol:protein length:13 Thrombin light chain
CGVPAIQPVLSGL
>1dlk_C mol:protein length:13 Thrombin light chain
CGVPAIQPVLSGL
>1dlk_B mol:protein length:230 Thrombin heavy chain
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
>1dlk_D mol:protein length:230 Thrombin heavy chain
IVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN
>1dlk_E mol:protein length:5 peptidic inhibitor
XGGFX
>1dlk_F mol:protein length:5 peptidic inhibitor
XGGFX |
4359 |
B7M1Y8 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B7M1Y8|ACCA_ECO8A Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O8 (strain IAI1) OX=585034 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4360 |
C4ZRS7 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|C4ZRS7|ACCA_ECOBW Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli (strain K12 / MC4100 / BW2952) OX=595496 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4360 |
1DLL |
PDB NFT |
The HC fragement of tetanus toxin complexed with lactose |
>1dll_A mol:protein length:441 TETANUS TOXIN
EDIDVILKKSTILNLDINNDIISDISGFNSSVITYPDAQLVPGINGKAIHLVNNESSEVIVHKAMDIEYNDMFNNFTVSFWLRVPKVSASHLEQYGTNEYSIISSMKKHSLSIGSGWSVSLKGNNLIWTLKDSAGEVRQITFRDLPDKFNAYLANKWVFITITNDRLSSANLYINGVLMGSAEITGLGAIREDNNITLKLDRCNNNNQYVSIDKFRIFCKALNPKEIEKLYTSYLSITFLRDFWGNPLRYDTEYYLIPVASSSKDVQLKNITDYMYLTNAPSYTNGKLNIYYRRLYNGLKFIIKRYTPNNEIDSFVKSGDFIKLYVSYNNNEHIVGYPKDGNAFNNLDRILRVGYNAPGIPLYKKMEAVKLRDLKTYSVQLKLYDDKNASLGLVGTHNGQIGNDPNRDILIASNWYFNHLKDKILGCDWYFVPTDEGWTND |
4360 |
HLA04539 B*37:21 |
HLA NFT |
B*37:21 |
>HLA:HLA04539 B*37:21 181 bp SHSMRYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYWDRETQIFKTNTQTYREDLRTLLRYYNQSEAGSHTIQRMSGCDVGPDGRLLRGYNQFAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQDRAYLEGTCVEWLRRYLENGKETLQRA |
4361 |
HLA04540 B*44:96 |
HLA NFT |
B*44:96 |
>HLA:HLA04540 B*44:96 181 bp SHSMRYFYTAMSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRENLRTALRYYNQSEAGSHIIQGMYGCDVGPDGRLLRGYDQDAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGLCVESLRRYLENGKETLQRA |
4361 |
1DLM |
PDB NFT |
STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER CALCOACETICUS NATIVE DATA |
>1dlm_A mol:protein length:311 CATECHOL 1,2-DIOXYGENASE
MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV
>1dlm_B mol:protein length:311 CATECHOL 1,2-DIOXYGENASE
MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV |
4361 |
B1XD54 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B1XD54|ACCA_ECODH Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli (strain K12 / DH10B) OX=316385 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4362 |
A7ZWD1 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|A7ZWD1|ACCA_ECOHS Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O9:H4 (strain HS) OX=331112 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4362 |
1DLO |
PDB NFT |
HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 |
>1dlo_A mol:protein length:556 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 REVERSE TRANSCRIPTASE
PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLSKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGI
>1dlo_B mol:protein length:427 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 REVERSE TRANSCRIPTASE
PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLSKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWY |
4362 |
HLA04541 B*44:97 |
HLA NFT |
B*44:97 |
>HLA:HLA04541 B*44:97 181 bp SHSMRYFYTAMSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQICKAKAQTDRENLRTALRYYNQSEAGSHIIQRMYGCDVGPDGRLLRGYDQDAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQDRAYLEGLCVESLRRYLENGKETLQRA |
4363 |
HLA04542 B*44:98 |
HLA NFT |
B*44:98 |
>HLA:HLA04542 B*44:98 181 bp SHSMRYFYTAMSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRENLRTALRYYNQSEAGSHIIQRMYGCDVGSDGRLLRGYDQDAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGLCVESLRRYLENGKETLQRA |
4363 |
1DLP |
PDB NFT |
STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN |
>1dlp_A mol:protein length:236 LECTIN SCAFET PRECURSOR
NNILFGLSHEGSHPQTLHAAQSLELSSFRFTMQSDCNLVLFDSDVRVWASNTAGATGCRAVLQSDGLLVILTAQNTIRWSSGTKGSIGNYVLVLQPDRTVTIYGPGLWDSGTSNKGSVVVANNGNSILYSTQGNDNHPQTLHATQSLQLSPYRLSMETDCNLVLFDRDDRVWSTNTAGKGTGCRAVLQPNGRMDVLTNQNIAVWTSGNSRSAGRYVFVLQPDRNLAIYGGALWTTG
>1dlp_B mol:protein length:236 LECTIN SCAFET PRECURSOR
NNILFGLSHEGSHPQTLHAAQSLELSSFRFTMQSDCNLVLFDSDVRVWASNTAGATGCRAVLQSDGLLVILTAQNTIRWSSGTKGSIGNYVLVLQPDRTVTIYGPGLWDSGTSNKGSVVVANNGNSILYSTQGNDNHPQTLHATQSLQLSPYRLSMETDCNLVLFDRDDRVWSTNTAGKGTGCRAVLQPNGRMDVLTNQNIAVWTSGNSRSAGRYVFVLQPDRNLAIYGGALWTTG
>1dlp_C mol:protein length:236 LECTIN SCAFET PRECURSOR
NNILFGLSHEGSHPQTLHAAQSLELSSFRFTMQSDCNLVLFDSDVRVWASNTAGATGCRAVLQSDGLLVILTAQNTIRWSSGTKGSIGNYVLVLQPDRTVTIYGPGLWDSGTSNKGSVVVANNGNSILYSTQGNDNHPQTLHATQSLQLSPYRLSMETDCNLVLFDRDDRVWSTNTAGKGTGCRAVLQPNGRMDVLTNQNIAVWTSGNSRSAGRYVFVLQPDRNLAIYGGALWTTG
>1dlp_D mol:protein length:236 LECTIN SCAFET PRECURSOR
NNILFGLSHEGSHPQTLHAAQSLELSSFRFTMQSDCNLVLFDSDVRVWASNTAGATGCRAVLQSDGLLVILTAQNTIRWSSGTKGSIGNYVLVLQPDRTVTIYGPGLWDSGTSNKGSVVVANNGNSILYSTQGNDNHPQTLHATQSLQLSPYRLSMETDCNLVLFDRDDRVWSTNTAGKGTGCRAVLQPNGRMDVLTNQNIAVWTSGNSRSAGRYVFVLQPDRNLAIYGGALWTTG
>1dlp_E mol:protein length:236 LECTIN SCAFET PRECURSOR
NNILFGLSHEGSHPQTLHAAQSLELSSFRFTMQSDCNLVLFDSDVRVWASNTAGATGCRAVLQSDGLLVILTAQNTIRWSSGTKGSIGNYVLVLQPDRTVTIYGPGLWDSGTSNKGSVVVANNGNSILYSTQGNDNHPQTLHATQSLQLSPYRLSMETDCNLVLFDRDDRVWSTNTAGKGTGCRAVLQPNGRMDVLTNQNIAVWTSGNSRSAGRYVFVLQPDRNLAIYGGALWTTG
>1dlp_F mol:protein length:236 LECTIN SCAFET PRECURSOR
NNILFGLSHEGSHPQTLHAAQSLELSSFRFTMQSDCNLVLFDSDVRVWASNTAGATGCRAVLQSDGLLVILTAQNTIRWSSGTKGSIGNYVLVLQPDRTVTIYGPGLWDSGTSNKGSVVVANNGNSILYSTQGNDNHPQTLHATQSLQLSPYRLSMETDCNLVLFDRDDRVWSTNTAGKGTGCRAVLQPNGRMDVLTNQNIAVWTSGNSRSAGRYVFVLQPDRNLAIYGGALWTTG |
4363 |
A1A7M9 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|A1A7M9|ACCA_ECOK1 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O1:K1 / APEC OX=405955 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLTDLADLDVLSTEDLKNRRYQRLMSYGYA |
4364 |
Q0TLE8 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|Q0TLE8|ACCA_ECOL5 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O6:K15:H31 (strain 536 / UPEC) OX=362663 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLGVPVVCTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4364 |
1DLQ |
PDB NFT |
STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 INHIBITED BY BOUND MERCURY |
>1dlq_A mol:protein length:311 CATECHOL 1,2-DIOXYGENASE
MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV
>1dlq_B mol:protein length:311 CATECHOL 1,2-DIOXYGENASE
MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV |
4364 |
HLA04543 B*40:02:08 |
HLA NFT |
B*40:02:08 |
>HLA:HLA04543 B*40:02:08 181 bp SHSMRYFHTSVSRPGRGEPRFITVGYVDDTLFVRFDSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRESLRNLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAARVAEQLRAYLEGECVEWLRRYLENGKETLQRA |
4365 |
HLA04544 B*35:01:19 |
HLA NFT |
B*35:01:19 |
>HLA:HLA04544 B*35:01:19 181 bp SHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYWDRNTQIFKTNTQTYRESLRNLRGYYNQSEAGSHIIQRMYGCDLGPDGRLLRGHDQSAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGLCVEWLRRYLENGKETLQRA |
4365 |
1DLR |
PDB NFT |
METHOTREXATE-RESISTANT VARIANTS OF HUMAN DIHYDROFOLATE REDUCTASE WITH SUBSTITUTION OF LEUCINE 22: KINETICS, CRYSTALLOGRAPHY AND POTENTIAL AS SELECTABLE MARKERS |
>1dlr_A mol:protein length:186 DIHYDROFOLATE REDUCTASE
VGSLNCIVAVSQNMGIGKNGDFPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND |
4365 |
Q8FL03 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|Q8FL03|ACCA_ECOL6 Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLSVPTICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4366 |
B1IQF6 |
AF NFT |
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha |
>sp|B1IQF6|ACCA_ECOLC Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha OS=Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks) OX=481805 GN=accA PE=3 SV=1 MSLNFLDFEQPIAELEAKIDSLTAVSRQDEKLDINIDEEVHRLREKSVELTRKIFADLGAWQIAQLARHPQRPYTLDYVRLAFDEFDELAGDRAYADDKAIVGGIARLDGRPVMIIGHQKGRETKEKIRRNFGMPAPEGYRKALRLMQMAERFKMPIITFIDTPGAYPGVGAEERGQSEAIARNLREMSRLSVPTICTVIGEGGSGGALAIGVGDKVNMLQYSTYSVISPEGCASILWKSADKAPLAAEAMGIIAPRLKELKLIDSIIPEPLGGAHRNPEAMAASLKAQLLADLADLDVLSTEDLKNRRYQRLMSYGYA |
4366 |
1DLS |
PDB NFT |
METHOTREXATE-RESISTANT VARIANTS OF HUMAN DIHYDROFOLATE REDUCTASE WITH SUBSTITUTION OF LEUCINE 22: KINETICS, CRYSTALLOGRAPHY AND POTENTIAL AS SELECTABLE MARKERS |
>1dls_A mol:protein length:186 DIHYDROFOLATE REDUCTASE
VGSLNCIVAVSQNMGIGKNGDYPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND |
4366 |
HLA04545 A*68:02:03 |
HLA NFT |
A*68:02:03 |
>HLA:HLA04545 A*68:02:03 181 bp SHSMRYFYTSMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDRNTRNVKAQSQTDRVDLGTLRGYYNQSEAGSHTIQRMYGCDVGPDGRFLRGYHQYAYDGKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQWRAYLEGTCVEWLRRYLENGKETLQRT |
4367 |
HLA04546 A*01:51 |
HLA NFT |
A*01:51 |
>HLA:HLA04546 A*01:51 181 bp SHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQKMEPRAPWIEQEGPEYWDRNTRNVKAHSQTDRANLGTLRGYYNQSEDGSHTIQIMYGCDVGPDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQRRVYLEGRCVDGLRRYLENGKETLQRT |
4367 |
1DLT |
PDB NFT |
STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 WITH BOUND CATECHOL |
>1dlt_A mol:protein length:311 CATECHOL 1,2-DIOXYGENASE
MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV
>1dlt_B mol:protein length:311 CATECHOL 1,2-DIOXYGENASE
MEVKIFNTQDVQDFLRVASGLEQEGGNPRVKQIIHRVLSDLYKAIEDLNITSDEYWAGVAYLNQLGANQEAGLLSPGLGFDHYLDMRMDAEDAALGIENATPRTIEGPLYVAGAPESVGYARMDDGSDPNGHTLILHGTIFDADGKPLPNAKVEIWHANTKGFYSHFDPTGEQQAFNMRRSIITDENGQYRVRTILPAGYGCPPEGPTQQLLNQLGRHGNRPAHIHYFVSADGHRKLTTQINVAGDPYTYDDFAYATREGLVVDAVEHTDPEAIKANDVEGPFAEMVFDLKLTRLVDGVDNQVVDRPRLAV |