P08191Uniprot
Fold
Class
Family
Origin
Species
Available structures
1TR7 : butyl a-d- mannopyranoside1UWF : butyl a-d- mannopyranoside2VCO : Mana13(Mana16)Manb14GlcNAcb14G3ZL1 : Thiazolyl mannoside3ZL2 : Thiazolyl mannoside4ATT : propynyl p-methoxy phenyl mann4AUJ : p-hydroxypropargyl phenyl mann4AUU : no ligand4AUY : a-p-hydroxypropynyl-phenyl man4AV0 : a-propynyl-p-methoxy-phenyl ma4AV4 : a-O-propynyl pyridine mannosid4AV5 : a-propynyl-biphenyl mannoside4AVH : a-propyl-thio-propyloyl mannos4AVI : a-methyl ester octyl mannoside4AVJ : a-methanol triazol ethyl pheny4AVK : a-propynyl-pyridine mannoside4CSS : sulfonamide biphenyl mannoside4CST : no ligand4LOV : Heptyl mannoside4X50 : biphenyl a-D-mannopyranoside4X5P : benzoyl-amidophenyl a-D-mannop4X5Q : 5-nitro-indolinylphenyl a-D-ma4X5R : squaryl-phenyl a-D-mannopyrano4XO8 : heptyl mannoside4XO9 : no ligand4XOA : no ligand4XOB : heptyl mannoside4XOD : no ligand5AB1 : beta-cyclodextrin C-linked alp5ABZ : C-mannoside derivative5F2F : Mannoside derivative5F3F : C-mannoside derivative5FS5 : n-heptyl a-D-mannopyrannoside5FWR : biphenyl-4-yl alpha-D-mannopyr5JCQ : no ligand5JCR : aManOMe5L4T : no ligand5L4U : no ligand5L4V : no ligand5L4W : no ligand5L4X : no ligand5L4Y : no ligand5MCA : no ligand5MTS : Thiazolylaminomannoside5MUC : 1,5-Anhydromannitol7AYN : Synthetic mannose derivative7BHD : core-fucosylated Man3Gn28BVD : Synthetic mannose derivative8BXY : alpha1,6 core-fucosylated olig8BY3 : Oligomannose-6
Related proteins
> 50% identity
> 50% identity
PubMed
Mousavifar L, Sarshar M, Bridot C, Scribano D, Ambrosi C, Palamara A, Vergoten G, Roubinet B, Landemarre L, Bouckaert J, Roy R.
Insightful Improvement in the Design of Potent Uropathogenic E. coli FimH Antagonists. Pharmaceutics 2023
Insightful Improvement in the Design of Potent Uropathogenic E. coli FimH Antagonists. Pharmaceutics 2023
PubMed
Krammer E, Bridot C, Serna S, Echeverria B, Semwal S, Roubinet B, van Noort K, Wilbers R, Bourenkov G, de Ruyck J, Landemarre L, Reichardt N, Bouckaert J.
Structural insights into a cooperative switch between one and two FimH bacterial adhesins binding pauci- and high-mannose type N-glycan receptors. The Journal of biological chemistry 2023
Structural insights into a cooperative switch between one and two FimH bacterial adhesins binding pauci- and high-mannose type N-glycan receptors. The Journal of biological chemistry 2023
PubMed
Krammer E, Bridot C, Serna S, Echeverria B, Semwal S, Roubinet B, van Noort K, Wilbers R, Bourenkov G, de Ruyck J, Landemarre L, Reichardt N, Bouckaert J.
Structural insights into a cooperative switch between one and two FimH bacterial adhesins binding pauci- and high-mannose type N-glycan receptors. The Journal of biological chemistry 2023
Structural insights into a cooperative switch between one and two FimH bacterial adhesins binding pauci- and high-mannose type N-glycan receptors. The Journal of biological chemistry 2023
PubMed
Tomasic T, Rabbani S, Jakob R, Reisner A, Jakopin Z, Maier T, Ernst B, Anderluh M.
Does targeting Arg98 of FimH lead to high affinity antagonists? European journal of medicinal chemistry 2021
Does targeting Arg98 of FimH lead to high affinity antagonists? European journal of medicinal chemistry 2021
PubMed
Zihlmann P, Silbermann M, Sharpe T, Jiang X, Mühlethaler T, Jakob R, Rabbani S, Sager C, Frei P, Pang L, Maier T, Ernst B.
KinITC-One Method Supports both Thermodynamic and Kinetic SARs as Exemplified on FimH Antagonists. Chemistry (Weinheim an der Bergstrasse, Germany) 2018
KinITC-One Method Supports both Thermodynamic and Kinetic SARs as Exemplified on FimH Antagonists. Chemistry (Weinheim an der Bergstrasse, Germany) 2018
PubMed
Zihlmann P, Silbermann M, Sharpe T, Jiang X, Mühlethaler T, Jakob R, Rabbani S, Sager C, Frei P, Pang L, Maier T, Ernst B.
KinITC-One Method Supports both Thermodynamic and Kinetic SARs as Exemplified on FimH Antagonists. Chemistry (Weinheim an der Bergstrasse, Germany) 2018
KinITC-One Method Supports both Thermodynamic and Kinetic SARs as Exemplified on FimH Antagonists. Chemistry (Weinheim an der Bergstrasse, Germany) 2018
PubMed
Rabbani S, Fiege B, Eris D, Silbermann M, Jakob R, Navarra G, Maier T, Ernst B.
Conformational switch of the bacterial adhesin FimH in the absence of the regulatory domain: Engineering a minimalistic allosteric system. The Journal of biological chemistry 2018
Conformational switch of the bacterial adhesin FimH in the absence of the regulatory domain: Engineering a minimalistic allosteric system. The Journal of biological chemistry 2018
PubMed
Rabbani S, Krammer E, Roos G, Zalewski A, Preston R, Eid S, Zihlmann P, Prévost M, Lensink M, Thompson A, Ernst B, Bouckaert J.
Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding. IUCrJ 2017
Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding. IUCrJ 2017
PubMed
Rabbani S, Krammer E, Roos G, Zalewski A, Preston R, Eid S, Zihlmann P, Prévost M, Lensink M, Thompson A, Ernst B, Bouckaert J.
Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding. IUCrJ 2017
Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding. IUCrJ 2017
PubMed
Alvarez Dorta D, Chalopin T, Sivignon A, de Ruyck J, Dumych T, Bilyy R, Deniaud D, Barnich N, Bouckaert J, Gouin S.
Physiochemical Tuning of Potent Escherichia coli Anti-Adhesives by Microencapsulation and Methylene Homologation. ChemMedChem 2017
Physiochemical Tuning of Potent Escherichia coli Anti-Adhesives by Microencapsulation and Methylene Homologation. ChemMedChem 2017
PubMed
Sauer M, Jakob R, Eras J, Baday S, Eris D, Navarra G, Bernèche S, Ernst B, Maier T, Glockshuber R.
Catch-bond mechanism of the bacterial adhesin FimH. Nature communications 2016
Catch-bond mechanism of the bacterial adhesin FimH. Nature communications 2016
PubMed
Sauer M, Jakob R, Eras J, Baday S, Eris D, Navarra G, Bernèche S, Ernst B, Maier T, Glockshuber R.
Catch-bond mechanism of the bacterial adhesin FimH. Nature communications 2016
Catch-bond mechanism of the bacterial adhesin FimH. Nature communications 2016
PubMed
Sauer M, Jakob R, Eras J, Baday S, Eris D, Navarra G, Bernèche S, Ernst B, Maier T, Glockshuber R.
Catch-bond mechanism of the bacterial adhesin FimH. Nature communications 2016
Catch-bond mechanism of the bacterial adhesin FimH. Nature communications 2016
PubMed
Sauer M, Jakob R, Eras J, Baday S, Eris D, Navarra G, Bernèche S, Ernst B, Maier T, Glockshuber R.
Catch-bond mechanism of the bacterial adhesin FimH. Nature communications 2016
Catch-bond mechanism of the bacterial adhesin FimH. Nature communications 2016
PubMed
Sauer M, Jakob R, Eras J, Baday S, Eris D, Navarra G, Bernèche S, Ernst B, Maier T, Glockshuber R.
Catch-bond mechanism of the bacterial adhesin FimH. Nature communications 2016
Catch-bond mechanism of the bacterial adhesin FimH. Nature communications 2016
PubMed
de Ruyck J, Lensink M, Bouckaert J.
Structures of C-mannosylated anti-adhesives bound to the type 1 fimbrial FimH adhesin. IUCrJ 2016
Structures of C-mannosylated anti-adhesives bound to the type 1 fimbrial FimH adhesin. IUCrJ 2016
PubMed
Jarvis C, Han Z, Kalas V, Klein R, Pinkner J, Ford B, Binkley J, Cusumano C, Cusumano Z, Mydock-McGrane L, Hultgren S, Janetka J.
Antivirulence Isoquinolone Mannosides: Optimization of the Biaryl Aglycone for FimH Lectin Binding Affinity and Efficacy in the Treatment of Chronic UTI. ChemMedChem 2016
Antivirulence Isoquinolone Mannosides: Optimization of the Biaryl Aglycone for FimH Lectin Binding Affinity and Efficacy in the Treatment of Chronic UTI. ChemMedChem 2016
PubMed
Mydock-McGrane L, Cusumano Z, Han Z, Binkley J, Kostakioti M, Hannan T, Pinkner J, Klein R, Kalas V, Crowley J, Rath N, Hultgren S, Janetka J.
Antivirulence C-Mannosides as Antibiotic-Sparing, Oral Therapeutics for Urinary Tract Infections. Journal of medicinal chemistry 2016
Antivirulence C-Mannosides as Antibiotic-Sparing, Oral Therapeutics for Urinary Tract Infections. Journal of medicinal chemistry 2016
PubMed
Fiege, B., Rabbani, S., Preston, R.C., Jakob, R.P., Zihlmann, P., Schwardt, O., Jiang, X., Maier, T., Ernst, B.
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
PubMed
Fiege, B., Rabbani, S., Preston, R.C., Jakob, R.P., Zihlmann, P., Schwardt, O., Jiang, X., Maier, T., Ernst, B.
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
PubMed
Fiege, B., Rabbani, S., Preston, R.C., Jakob, R.P., Zihlmann, P., Schwardt, O., Jiang, X., Maier, T., Ernst, B.
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
PubMed
Fiege, B., Rabbani, S., Preston, R.C., Jakob, R.P., Zihlmann, P., Schwardt, O., Jiang, X., Maier, T., Ernst, B.
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
PubMed
Fiege, B., Rabbani, S., Preston, R.C., Jakob, R.P., Zihlmann, P., Schwardt, O., Jiang, X., Maier, T., Ernst, B.
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
PubMed
Fiege, B., Rabbani, S., Preston, R.C., Jakob, R.P., Zihlmann, P., Schwardt, O., Jiang, X., Maier, T., Ernst, B.
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ChemBioChem 2015
PubMed
Vanwetswinkel S, Volkov A, Sterckx Y, Garcia-Pino A, Buts L, Vranken W, Bouckaert J, Roy R, Wyns L, van Nuland N.
Study of the structural and dynamic effects in the FimH adhesin upon alpha-d-heptyl mannose binding. Journal of medicinal chemistry 2014
Study of the structural and dynamic effects in the FimH adhesin upon alpha-d-heptyl mannose binding. Journal of medicinal chemistry 2014
PubMed
Brument, S., Sivignon, A., Dumych, T.I., Moreau, N., Roos, G., Guerardel, Y., Chalopin, T., Deniaud, D., Bilyy, R.O., Darfeuille-Michaud, A., Bouckaert, J., Gouin, S.G.
Thiazolylaminomannosides as potent antiadhesives of type 1 piliated Escherichia coli isolated from Crohn's disease patients. J. Med. Chem. 2013
Thiazolylaminomannosides as potent antiadhesives of type 1 piliated Escherichia coli isolated from Crohn's disease patients. J. Med. Chem. 2013
PubMed
Brument, S., Sivignon, A., Dumych, T.I., Moreau, N., Roos, G., Guerardel, Y., Chalopin, T., Deniaud, D., Bilyy, R.O., Darfeuille-Michaud, A., Bouckaert, J., Gouin, S.G.
Thiazolylaminomannosides as potent antiadhesives of type 1 piliated Escherichia coli isolated from Crohn's disease patients. J. Med. Chem. 2013
Thiazolylaminomannosides as potent antiadhesives of type 1 piliated Escherichia coli isolated from Crohn's disease patients. J. Med. Chem. 2013
PubMed
Roos, G., Wellens, A., Touaibia, M., Yamakawa, N., Geerlings, P., Roy, R., Wyns, L., Bouchaert, J.
Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of FimH. ACS Med. Chem. Lett. 2013
Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of FimH. ACS Med. Chem. Lett. 2013
PubMed
Roos, G., Wellens, A., Touaibia, M., Yamakawa, N., Geerlings, P., Roy, R., Wyns, L., Bouchaert, J.
Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of FimH. ACS Med. Chem. Lett. 2013
Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of FimH. ACS Med. Chem. Lett. 2013
PubMed
Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J.
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
PubMed
Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J.
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
PubMed
Oscarson S, Roy R, Remaut H, Bouckaert J.
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
PubMed
Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J.
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
PubMed
Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J.
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
PubMed
Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J.
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
PubMed
Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J.
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
PubMed
Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J.
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
PubMed
Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J.
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
The tyrosine gate as a potential entropic lever in the receptor-binding site of the bacterial adhesin FimH. Biochemistry 2012
PubMed
Wellens A, Garofalo C, Nguyen H, Van Gerven N, Slattegard R, Hernalsteens JP, Wyns L, Oscarson S, De Greve H, Hultgren S, Bouckaert J
Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex PLoS ONE 2008
Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex PLoS ONE 2008
PubMed
Wellens A, Garofalo C, Nguyen H, Van Gerven N, Slattegard R, Hernalsteens J, Wyns L, Oscarson S, De Greve H, Hultgren S, Bouckaert J.
Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex. PloS one 2008
Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex. PloS one 2008
PubMed
Bouckaert J, Berglund J, Schembri M, De Genst E, Cools L, Wuhrer M, Hung CS, Pinkner J, Slattegard R, Zavialov A, Choudhury D, Langermann S, Hultgren
Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin Mol. Microbiol. 2005
Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin Mol. Microbiol. 2005
PubMed
Bouckaert J, Berglund J, Schembri M, De Genst E, Cools L, Wuhrer M, Hung CS, Pinkner J, Slattegard R, Zavialov A, Choudhury D, Langermann S, Hultgren
Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin Mol. Microbiol. 2005
Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin Mol. Microbiol. 2005
PubMed
Jakob, R.P., Rabbani, S., Ernst, B., Maier, T.
Crystal structure of the FimH lectin domain from E.coli K12 in complex with methyl alpha-D-mannopyrannoside in spacegroup P21 To be published. 0
Crystal structure of the FimH lectin domain from E.coli K12 in complex with methyl alpha-D-mannopyrannoside in spacegroup P21 To be published. 0
PubMed
Zihlmann, P., Jiang, X., Sager, C.P., Fiege, B., Jakob, R.P., Siegrist, S., Zalewski, A., Rabbani, S., Eris, D., Silbermann, M., Pang, L., Muhlethaler, T., Sharpe, T., Maier, T., Ernst, B.
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
PubMed
Zihlmann, P., Jiang, X., Sager, C.P., Fiege, B., Jakob, R.P., Siegrist, S., Zalewski, A., Rabbani, S., Eris, D., Silbermann, M., Pang, L., Muhlethaler, T., Sharpe, T., Maier, T., Ernst, B.
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
PubMed
Zihlmann, P., Jiang, X., Sager, C.P., Fiege, B., Jakob, R.P., Siegrist, S., Zalewski, A., Rabbani, S., Eris, D., Silbermann, M., Pang, L., Muhlethaler, T., Sharpe, T., Maier, T., Ernst, B.
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
PubMed
Zihlmann, P., Jiang, X., Sager, C.P., Fiege, B., Jakob, R.P., Siegrist, S., Zalewski, A., Rabbani, S., Eris, D., Silbermann, M., Pang, L., Muhlethaler, T., Sharpe, T., Maier, T., Ernst, B.
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
PubMed
Zihlmann, P., Jiang, X., Sager, C.P., Fiege, B., Jakob, R.P., Siegrist, S., Zalewski, A., Rabbani, S., Eris, D., Silbermann, M., Pang, L., Muhlethaler, T., Sharpe, T., Maier, T., Ernst, B.
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
PubMed
Zihlmann, P., Jiang, X., Sager, C.P., Fiege, B., Jakob, R.P., Siegrist, S., Zalewski, A., Rabbani, S., Eris, D., Silbermann, M., Pang, L., Muhlethaler, T., Sharpe, T., Maier, T., Ernst, B.
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
PubMed
Zihlmann, P., Jiang, X., Sager, C.P., Fiege, B., Jakob, R.P., Siegrist, S., Zalewski, A., Rabbani, S., Eris, D., Silbermann, M., Pang, L., Muhlethaler, T., Sharpe, T., Maier, T., Ernst, B.
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
High-Affinity Carbohydrate-Lectin Interactions: How Nature Makes it Possible To be published. 0
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