DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structures of glyceraldehyde 3-phosphate dehydrogenase in Neisseria gonorrhoeae and Chlamydia trachomatis. Structures of glyceraldehyde 3-phosphate dehydrogenase in Neisseria gonorrhoeae and Chlamydia trachomatis. Protein science : a publication of the Protein Society 2020 imex curation Barrett KF., Dranow DM., Phan IQ., Michaels SA., Shaheen S., Navaluna ED., Craig JK., Tillery LM., Choi R., Edwards TE., Conrady DG., Abendroth J., Horanyi PS., Lorimer DD., Van Voorhis WC., Zhang Z., Barrett LK., Subramanian S., Staker B., Fan E., Myler PJ., Soge OO., Hybiske K., Ojo KK. ojo67kk@uw.edu Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Barrett KF., Dranow DM., Phan IQ., Michaels SA., Shaheen S., Navaluna ED., Craig JK., Tillery LM., Choi R., Edwards TE., Conrady DG., Abendroth J., Horanyi PS., Lorimer DD., Van Voorhis WC., Zhang Z., Barrett LK., Subramanian S., Staker B., Fan E., Myler PJ., Soge OO., Hybiske K., Ojo KK. ojo67kk@uw.edu Accepted 2021-DEC-20 AT 05:50 GMT AT 05:50 GMT by KALPANAP Protein science : a publication of the Protein Society 2020 Only protein-protein interactions imex curation imex curation b4rpp8_neig2 Glyceraldehyde-3-phosphate dehydrogenase NGK_2321 protein protein Neisseria gonorrhoeae (strain NCCP11945) Neisseria gonorrhoeae (strain NCCP11945) MECSFISEYNTGIGLYFTTGRQNMSIKVAINGFGRIGRLALRQIEKAHGIEVAAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGREIKVFANPNPEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAASCTTNCLAPMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRKGDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVATGSLTELVSVLERPATKEEINAAMKAASSESYGYNEDQIVSSDVVGIEYGSLFDATQTRVMTVGGKQLVKTVAWYDNEMSYTCQLVRTLEYFAGKI 66B7D7F77143A93C g3p_chltr Glyceraldehyde-3-phosphate dehydrogenase gap gapA CT_505 NAD-dependent glyceraldehyde-3-phosphate dehydrogenase protein protein chltr chltr MRIVINGFGRIGRLVLRQILKRNSPIEVVAINDLVAGDLLTYLFKYDSTHGSFAPQATFSDGCLVMGERKVHFLAEKDVQKLPWKDLDVDVVVESTGLFVNRDDVAKHLDSGAKRVLITAPAKGDVPTFVMGVNHQQFDPADVIISNASCTTNCLAPLAKVLLDNFGIEEGLMTTVHAATATQSVVDGPSRKDWRGGRGAFQNIIPASTGAAKAVGLCLPELKGKLTGMAFRVPVADVSVVDLTVKLSSATTYEAICEAVKHAANTSMKNIMYYTEEAVVSSDFIGCEYSSVFDAQAGVALNDRFFKLVAWYDNEIGYATRIVDLLEYVQENSK 3F4DEED6F073ADCD b4rpp8_neig2-1 1 2 unspecified role unspecified role neutral component neutral component purified purified B4RPP8:p.[Ala81del;Thr234del] mutation mutation certain certain sequence position certain certain certain sequence position certain A . certain certain sequence position certain certain certain sequence position certain T . His tag His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range binding region binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) physical association physical association Fig 1, Table 4-6 gap-4 1 3 unspecified role unspecified role neutral component neutral component purified purified His tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range binding region binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P0CE13:p.[His72Arg;Val105Ala] p.[H72R;V105A] mutation mutation certain certain sequence position certain certain certain sequence position certain V A certain certain sequence position certain certain certain sequence position certain H R ecoli Escherichia coli (strain K12) physical association physical association Fig 1, Table 4-6