IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition. Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition. Protein Sci. (0961-8368) 2012 imex curation Johnson E., Nguyen P.T., Yeates T.O., Rees D.C. Margaret: Before you are looking for a needle in the haystack: There are three crystal structures: 3tui: native, purified in buffer containing CY5, crystallized with ATP - 3tuj: expressed in selenomethionine-containing medium, purified in buffer containing DM, crystallized without ATP - 3tuz: expressed natively, purified in buffer containing CY5, crystallized with ATP, soaked in selenomethionine solution - It appears that 2 crystals mentioned in the methods did not provide good enough resolution to be considered in the main paper: 1. crystal containing MetI, MetN AND MetQ with ATP. - 2. CY5 crystal expressed in selenomethionine-containing. - Also: Although crystals were produced in buffer containing ATP, modelling of the ligand resulted in ADP being the most likely ligand actually found in the crystal. Should this be a comment? Additional methods are in Ref. 9: pmid: 18621668 (which you also have for checking!) dcrees@caltech.edu 28-Oct_2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Johnson E., Nguyen P.T., Yeates T.O., Rees D.C. Margaret: Before you are looking for a needle in the haystack: There are three crystal structures: 3tui: native, purified in buffer containing CY5, crystallized with ATP - 3tuj: expressed in selenomethionine-containing medium, purified in buffer containing DM, crystallized without ATP - 3tuz: expressed natively, purified in buffer containing CY5, crystallized with ATP, soaked in selenomethionine solution - It appears that 2 crystals mentioned in the methods did not provide good enough resolution to be considered in the main paper: 1. crystal containing MetI, MetN AND MetQ with ATP. - 2. CY5 crystal expressed in selenomethionine-containing. - Also: Although crystals were produced in buffer containing ATP, modelling of the ligand resulted in ADP being the most likely ligand actually found in the crystal. Should this be a comment? Additional methods are in Ref. 9: pmid: 18621668 (which you also have for checking!) dcrees@caltech.edu Accepted 2013-OCT-14 by MGT 28-Oct_2013: Contacted by IntAct-Help. Protein Sci. (0961-8368) 2012 Only protein-protein interactions imex curation metn_ecoli Methionine import ATP-binding protein MetN metN abc b0199 JW0195 protein protein ecoli Escherichia coli (strain K12) MIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQQDTQAAIAWLQEHHVKVEVLGYV DIP protein P30750 original sequence version: 94 DIP protein P30750 original sequence version: null 2FC796C605216FB3 l-selenomethionine L-selenomethionine L-selenomethionine (2S)-2-amino-4-(methylseleno)butanoic acid small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) RJFAYQIBOAGBLC-BYPYZUCNSA-N RJFAYQIBOAGBLC-BYPYZUCNSA-N meti_ecoli D-methionine transport system permease protein MetI metI yaeE b0198 JW0194 protein protein ecoli Escherichia coli (strain K12) MSEPMMWLLVRGVWETLAMTFVSGFFGFVIGLPVGVLLYVTRPGQIIANAKLYRTVSAIVNIFRSIPFIILLVWMIPFTRVIVGTSIGLQAAIVPLTVGAAPFIARMVENALLEIPTGLIEASRAMGATPMQIVRKVLLPEALPGLVNAATITLITLVGYSAMGGAVGAGGLGQIGYQYGYIGYNATVMNTVLVLLVILVYLIQFAGDRIVRAVTRK DIP protein P31547 original sequence version: 80 EC1A22D772468EA8 adp adenosine 5'-(trihydrogen diphosphate) (ADP) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) meti-metn-adp-1 1 5 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 2 unspecified role unspecified role neutral component neutral component n-terminal 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 P30750:p.Glu166Gln mutation mutation certain certain sequence position certain certain certain sequence position certain E Q Wed May 02 20:09:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu166gln' Tue Jun 30 19:59:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu166Gln' ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction 2.9 A R = 0.24; Rwork = 0.24; Rfree = 0.3 purified in buffer containing CY5 Fig.s 1a-c, 2, 3, 4b, 7, S1b, S3-4, S5a meti-metn 1 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 2 unspecified role unspecified role neutral component neutral component n-terminal 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 P30750:p.Glu166Gln mutation mutation certain certain sequence position certain certain certain sequence position certain E Q Wed May 02 16:08:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu166gln' Tue Jun 30 19:01:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu166Gln' region se(s)met L-selenomethionine Delta:S(-1)Se(1) Se(S)Met Selenium replaces sulphur semetm undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction 4.0 A R = 0.26; Rwork = 0.26; Rfree = 0.3 purified in buffer containing DM Fig. 1d, 4b, 7, S5d meti-metn-adp-2 1 2 unspecified role unspecified role neutral component neutral component n-terminal 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 P30750:p.Glu166Gln mutation mutation certain certain sequence position certain certain certain sequence position certain E Q Wed May 02 18:36:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu166gln' Tue Jun 30 17:29:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu166Gln' ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) 3 unspecified role unspecified role neutral component neutral component chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction 3.4 A R = 0.26; Rwork = 0.26; Rfree = 0.31 Fig.s 4, 5, S1a, S5b, S6 purified in buffer containing CY5 SeMet soak