{"count":839,"next":"http://glycodata.org/api/gdd/glyco-properties/?format=json&page=3","previous":"http://glycodata.org/api/gdd/glyco-properties/?format=json","results":[{"id":21,"dataset":"carbohydrate","entity":"GM1 oligosaccharide (ganglioside GM1)","entity_group":"","entity_class":"oligosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.043","unit":"µM","value_reported":"43","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs cholera toxin B subunit (CTB), isothermal titration calorimetry (ITC)","conditions":"Kd vs cholera toxin B subunit (CTB), isothermal titration calorimetry (ITC)","conditions_detail":"Kd vs cholera toxin B subunit (CTB), isothermal titration calorimetry (ITC) | partner: cholera toxin B subunit (CTB) | technique: ITC","doi":"10.1021/acs.biomac.8b01736","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6429436/","year":"2019","confidence":"medium","comments":"\"The high-affinity binding interaction of GM1-CTB has a Kd of 43 nM, as demonstrated using isothermal titration calorimetry (ITC)\"  — Classic high-affinity glycan-protein interaction; 43 nM is the widely cited monovalent GM1 oligosaccharide-CTB Kd. Value obtained via search of this article; DOI is the article's.  [Heggelund JE, et al. (value as cited), 2019, confidence: medium]"},{"id":22,"dataset":"carbohydrate","entity":"2,6-sialyllactose (Neu5Ac-alpha2,6-Gal-Glc)","entity_group":"","entity_class":"sialic acid","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"2100","unit":"µM","value_reported":"2.1","unit_reported":"mM","method":"Experiment","method_detail":"Kd vs influenza X-31 hemagglutinin (human H3), 500-MHz proton NMR; 2,6-linked sialyllactose","conditions":"Kd vs influenza X-31 hemagglutinin (human H3), 500-MHz proton NMR; 2,6-linked sialyllactose","conditions_detail":"Kd vs influenza X-31 hemagglutinin (human H3), 500-MHz proton NMR; 2,6-linked sialyllactose | partner: influenza hemagglutinin (X-31, H3) | technique: NMR","doi":"10.1073/pnas.1120265109","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3427095/","year":"2012","confidence":"high","comments":"\"the dissociation constant of X-31 HA to sialyllactose was reported to be 2.1 mM (2,6 linked) and 3.2 mM (2,3 linked)\"  — Original NMR data from Sauter et al. 1992, Biochemistry 31:9609-9621 (DOI 10.1021/bi00447a018); cited here. Weak monovalent affinity; avidity from HA trimer multivalency.  [Sieben C, Kappel C, Zhu R, et al., 2012, confidence: high]"},{"id":23,"dataset":"carbohydrate","entity":"2,3-sialyllactose (Neu5Ac-alpha2,3-Gal-Glc)","entity_group":"","entity_class":"sialic acid","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"3200","unit":"µM","value_reported":"3.2","unit_reported":"mM","method":"Experiment","method_detail":"Kd vs influenza X-31 hemagglutinin (human H3), 500-MHz proton NMR; 2,3-linked sialyllactose","conditions":"Kd vs influenza X-31 hemagglutinin (human H3), 500-MHz proton NMR; 2,3-linked sialyllactose","conditions_detail":"Kd vs influenza X-31 hemagglutinin (human H3), 500-MHz proton NMR; 2,3-linked sialyllactose | partner: influenza hemagglutinin (X-31, H3) | technique: NMR","doi":"10.1073/pnas.1120265109","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3427095/","year":"2012","confidence":"high","comments":"\"the dissociation constant of X-31 HA to sialyllactose was reported to be 2.1 mM (2,6 linked) and 3.2 mM (2,3 linked)\"  — Original NMR data from Sauter et al. 1992. Weak monovalent affinity.  [Sieben C, Kappel C, Zhu R, et al., 2012, confidence: high]"},{"id":24,"dataset":"carbohydrate","entity":"L-fucose","entity_group":"","entity_class":"monosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"22000","unit":"µM","value_reported":"22","unit_reported":"mM","method":"Experiment","method_detail":"Kd vs norovirus GII.4 Saga P-dimer, chemical-shift-perturbation (CSP) NMR","conditions":"Kd vs norovirus GII.4 Saga P-dimer, chemical-shift-perturbation (CSP) NMR","conditions_detail":"Kd vs norovirus GII.4 Saga P-dimer, chemical-shift-perturbation (CSP) NMR | partner: norovirus GII.4 Saga P-dimer (VP1 protruding domain) | technique: NMR (CSP)","doi":"10.1042/BST20210526","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC9022987/","year":"2021","confidence":"high","comments":"\"l-fucose is a very weak binder with a dissociation constant of ... 22 mM\"  — L-fucose is the minimal HBGA binding element for human norovirus.  [Peters T, Creutznacher R, Maass T, et al., 2021, confidence: high]"},{"id":25,"dataset":"carbohydrate","entity":"H-disaccharide (alpha-L-Fuc-(1,2)-D-Gal)","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"30000","unit":"µM","value_reported":"30","unit_reported":"mM","method":"Experiment","method_detail":"Kd vs norovirus GII.4 Saga P-dimer, chemical-shift-perturbation (CSP) NMR","conditions":"Kd vs norovirus GII.4 Saga P-dimer, chemical-shift-perturbation (CSP) NMR","conditions_detail":"Kd vs norovirus GII.4 Saga P-dimer, chemical-shift-perturbation (CSP) NMR | partner: norovirus GII.4 Saga P-dimer (VP1 protruding domain) | technique: NMR (CSP)","doi":"10.1042/BST20210526","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC9022987/","year":"2021","confidence":"high","comments":"\"H-disaccharide is a very weak binder with a dissociation constant of 30 mM\"  — HBGA H-type epitope; GII.4 Saga strain.  [Peters T, Creutznacher R, Maass T, et al., 2021, confidence: high]"},{"id":26,"dataset":"carbohydrate","entity":"H-disaccharide (alpha-L-Fuc-(1,2)-D-Gal)","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"420","unit":"µM","value_reported":"420","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs norovirus GII.10 Vietnam P-dimer, STD NMR titration","conditions":"Kd vs norovirus GII.10 Vietnam P-dimer, STD NMR titration","conditions_detail":"Kd vs norovirus GII.10 Vietnam P-dimer, STD NMR titration | partner: norovirus GII.10 Vietnam P-dimer (VP1 protruding domain) | technique: STD NMR","doi":"10.1042/BST20210526","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC9022987/","year":"2021","confidence":"high","comments":"\"dissociation constants KD were given as follows ... 420 microM (H-disaccharide)\"  — Same H-disaccharide binds GII.10 Vietnam P-dimer ~70x more tightly than GII.4 Saga - strain-dependent affinity.  [Peters T, Creutznacher R, Maass T, et al., 2021, confidence: high]"},{"id":27,"dataset":"carbohydrate","entity":"H-disaccharide (alpha-L-Fuc-(1,2)-D-Gal)","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"2100","unit":"µM","value_reported":"2.1","unit_reported":"mM","method":"Experiment","method_detail":"Kd vs norovirus GII.4 VA387 P-dimer, native mass spectrometry; 2.1 and 1.5 mM for two P-dimer constructs","conditions":"Kd vs norovirus GII.4 VA387 P-dimer, native mass spectrometry; 2.1 and 1.5 mM for two P-dimer constructs","conditions_detail":"Kd vs norovirus GII.4 VA387 P-dimer, native mass spectrometry; 2.1 and 1.5 mM for two P-dimer constructs | partner: norovirus GII.4 VA387 P-dimer (VP1 protruding domain) | technique: native mass spectrometry","doi":"10.1042/BST20210526","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC9022987/","year":"2021","confidence":"high","comments":"\"dissociation constants KD of 2.1 and 1.5 mM were determined for two slightly different P-dimer constructs\"  — Native MS value; illustrates method/strain dependence of reported HBGA affinities.  [Peters T, Creutznacher R, Maass T, et al., 2021, confidence: high]"},{"id":28,"dataset":"carbohydrate","entity":"Neu5Ac-alpha2,6-LacNAc (Neu5Ac-alpha2,6-Gal-beta1,4-GlcNAc)","entity_group":"","entity_class":"sialic acid","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"100","unit":"µM","value_reported":"100","unit_reported":"uM","method":"Review","method_detail":"Kd vs CD22 (Siglec-2); affinity range 50-200 uM cited (midpoint 100 uM recorded)","conditions":"Kd vs CD22 (Siglec-2); affinity range 50-200 uM cited (midpoint 100 uM recorded)","conditions_detail":"Kd vs CD22 (Siglec-2); affinity range 50-200 uM cited (midpoint 100 uM recorded) | partner: CD22 (Siglec-2) | technique: compiled (Kimura 2007; Macauley 2015)","doi":"","source_url":"https://glycopedia.eu/echapter/article-introduction-3/article-cd22-siglec-2/","year":"2015","confidence":"medium","comments":"\"CD22 has a strong preference for alpha2-6 Sia ligands, in particular Neu5Acalpha2-6Galbeta1-4GlcNAc (Neu5Acalpha2-6LacNAc), with an affinity range between 50-200 microM\"  — Reported as range 50-200 uM; midpoint 100 uM recorded. Siglec-2/CD22 is alpha2,6-sialoside specific.  [Glycopedia (citing Kimura et al. 2007; Macauley et al. 2015), 2015, confidence: medium]"},{"id":29,"dataset":"carbohydrate","entity":"Tn-antigen porcine submaxillary mucin (terminal alpha-GalNAc)","entity_group":"","entity_class":"glycan (O-linked)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.0002","unit":"µM","value_reported":"0.2","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs soybean agglutinin (SBA), isothermal titration calorimetry (ITC); multivalent Tn-PSM, ~10^6-fold avidity enhancement vs monovalent GalNAc","conditions":"Kd vs soybean agglutinin (SBA), isothermal titration calorimetry (ITC); multivalent Tn-PSM, ~10^6-fold avidity enhancement vs monovalent GalNAc","conditions_detail":"Kd vs soybean agglutinin (SBA), isothermal titration calorimetry (ITC); multivalent Tn-PSM, ~10^6-fold avidity enhancement vs monovalent GalNAc | partner: soybean agglutinin (SBA) | technique: ITC","doi":"10.1074/jbc.M703119200","source_url":"https://www.sciencedirect.com/science/article/pii/S002192582058722X","year":"2007","confidence":"medium","comments":"\"Soybean agglutinin (SBA) binds to porcine submaxillary mucin with terminal alpha-GalNAc residues (Tn-PSM) with a Kd of 0.2 nM using isothermal titration microcalorimetry (ITC), which represents a ~10^6-fold enhanced affinity relative to monovalent GalNAcalpha1-O-Ser\"  — Extreme multivalent avidity (0.2 nM) of SBA for the high-density Tn-mucin; monovalent GalNAc affinity is ~10^6-fold weaker. Value obtained via search of this JBC article.  [Dam TK, Gerken TA, Cavada BS, et al., 2007, confidence: medium]"},{"id":30,"dataset":"carbohydrate","entity":"F3 (heparin-derived oligosaccharide)","entity_group":"","entity_class":"oligosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"3300","unit":"µM","value_reported":"3.3","unit_reported":"mM","method":"Experiment","method_detail":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 3.3 +/- 0.1 mM (TFS) / 2.5 +/- 0.1 mM by ITC, 25 C, PBS","conditions":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 3.3 +/- 0.1 mM (TFS) / 2.5 +/- 0.1 mM by ITC, 25 C, PBS","conditions_detail":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 3.3 +/- 0.1 mM (TFS) / 2.5 +/- 0.1 mM by ITC, 25 C, PBS | partner: galectin-3 | technique: intrinsic tryptophan fluorescence | temperature C: 25","doi":"10.1038/s41598-019-47658-8","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/","year":"2019","confidence":"high","comments":"\"dissociation constant of F3 binding to galectin-3 was determined to be KD, 3.3 +/- 0.1 mM\"  — Heparin-derived fragment binding to galectin-3; cross-validated with ITC (2.5 mM).  [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]"},{"id":31,"dataset":"carbohydrate","entity":"N-acetyllactosamine (LacNAc)","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"9300","unit":"µM","value_reported":"9.3","unit_reported":"mM","method":"Experiment","method_detail":"Kd vs human galectin-4 (full-length), intrinsic tryptophan fluorescence spectroscopy (TFS); 9.3 +/- 0.8 mM (TFS) / 3.5 +/- 0.5 mM by ITC, 25 C, PBS","conditions":"Kd vs human galectin-4 (full-length), intrinsic tryptophan fluorescence spectroscopy (TFS); 9.3 +/- 0.8 mM (TFS) / 3.5 +/- 0.5 mM by ITC, 25 C, PBS","conditions_detail":"Kd vs human galectin-4 (full-length), intrinsic tryptophan fluorescence spectroscopy (TFS); 9.3 +/- 0.8 mM (TFS) / 3.5 +/- 0.5 mM by ITC, 25 C, PBS | partner: galectin-4 | technique: intrinsic tryptophan fluorescence | temperature C: 25","doi":"10.1038/s41598-019-47658-8","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/","year":"2019","confidence":"medium","comments":"\"LacNAc bindings (KD, 7.4 +/- 0.9 mM, 12.1 +/- 0.7 mM, respectively)\"  — Full-length galectin-4 LacNAc TFS value 9.3 mM (galectin-4N 7.4 mM, galectin-4C 12.1 mM domains).  [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: medium]"},{"id":32,"dataset":"carbohydrate","entity":"lactose","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"1300","unit":"µM","value_reported":"1.3","unit_reported":"mM","method":"Experiment","method_detail":"Kd vs human galectin-2, intrinsic tryptophan fluorescence spectroscopy (TFS); 1.3 +/- 0.2 mM (TFS) / 960.5 +/- 179.5 uM by ITC, 25 C, PBS","conditions":"Kd vs human galectin-2, intrinsic tryptophan fluorescence spectroscopy (TFS); 1.3 +/- 0.2 mM (TFS) / 960.5 +/- 179.5 uM by ITC, 25 C, PBS","conditions_detail":"Kd vs human galectin-2, intrinsic tryptophan fluorescence spectroscopy (TFS); 1.3 +/- 0.2 mM (TFS) / 960.5 +/- 179.5 uM by ITC, 25 C, PBS | partner: galectin-2 | technique: intrinsic tryptophan fluorescence | temperature C: 25","doi":"10.1038/s41598-019-47658-8","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/","year":"2019","confidence":"high","comments":"\"The KD values of LacNAc, lactose and galactose binding to galectin-2 were 654.4 +/- 155.4 microM, 1.3 +/- 0.2 mM and 35.6 +/- 2.6 mM, respectively\"  — Cross-validated with ITC (960.5 uM).  [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]"},{"id":33,"dataset":"carbohydrate","entity":"Man9GlcNAc2 (high-mannose N-glycan)","entity_group":"","entity_class":"glycan (N-linked)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"26","unit":"µM","value_reported":"26","unit_reported":"uM","method":"Experiment","method_detail":"Inhibition constant Ki (not Kd) vs DC-SIGN CRD, 125I-Man-BSA solid-phase competition binding assay","conditions":"Inhibition constant Ki (not Kd) vs DC-SIGN CRD, 125I-Man-BSA solid-phase competition binding assay","conditions_detail":"Inhibition constant Ki (not Kd) vs DC-SIGN CRD, 125I-Man-BSA solid-phase competition binding assay | partner: DC-SIGN (CRD) | technique: solid-phase competition (radioligand)","doi":"10.1074/jbc.M609689200","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC2277367/","year":"2007","confidence":"medium","comments":"\"Solid phase competition binding assays were performed using bacterially expressed CRDs of DC-SIGN and DC-SIGNR, with 125I-Man-bovine serum albumin employed as the reporter ligand\"  — Value is a Ki (inhibition constant) from competition assay, NOT a true Kd. Man9GlcNAc2 Ki = 26 uM for DC-SIGN; recorded for completeness with this caveat.  [Feinberg H, Castelli R, Drickamer K, Seeberger PH, Weis WI, 2007, confidence: medium]"},{"id":34,"dataset":"carbohydrate","entity":"Man9 (oligomannose-9)","entity_group":"","entity_class":"oligosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"73","unit":"µM","value_reported":"73","unit_reported":"uM","method":"Experiment","method_detail":"Inhibition constant Ki (not Kd) vs DC-SIGN CRD, 125I-Man-BSA solid-phase competition binding assay; 73 +/- 6 uM","conditions":"Inhibition constant Ki (not Kd) vs DC-SIGN CRD, 125I-Man-BSA solid-phase competition binding assay; 73 +/- 6 uM","conditions_detail":"Inhibition constant Ki (not Kd) vs DC-SIGN CRD, 125I-Man-BSA solid-phase competition binding assay; 73 +/- 6 uM | partner: DC-SIGN (CRD) | technique: solid-phase competition (radioligand)","doi":"10.1074/jbc.M609689200","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC2277367/","year":"2007","confidence":"medium","comments":"\"Man9 | DC-SIGN | 73 +/- 6 microM | Solid-phase competition\"  — Ki from competition assay (not a direct Kd).  [Feinberg H, Castelli R, Drickamer K, Seeberger PH, Weis WI, 2007, confidence: medium]"},{"id":35,"dataset":"carbohydrate","entity":"mannose","entity_group":"","entity_class":"monosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"2300","unit":"µM","value_reported":"2300","unit_reported":"uM","method":"Experiment","method_detail":"Inhibition constant Ki (not Kd) vs DC-SIGN CRD, 125I-Man-BSA solid-phase competition binding assay; 2300 +/- 100 uM","conditions":"Inhibition constant Ki (not Kd) vs DC-SIGN CRD, 125I-Man-BSA solid-phase competition binding assay; 2300 +/- 100 uM","conditions_detail":"Inhibition constant Ki (not Kd) vs DC-SIGN CRD, 125I-Man-BSA solid-phase competition binding assay; 2300 +/- 100 uM | partner: DC-SIGN (CRD) | technique: solid-phase competition (radioligand)","doi":"10.1074/jbc.M609689200","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC2277367/","year":"2007","confidence":"medium","comments":"\"Mannose | DC-SIGN | 2300 +/- 100 microM | Solid-phase competition\"  — Monosaccharide mannose Ki = 2300 uM (weak); Ki not Kd. Affinity increases ~30-90x with oligomannose.  [Feinberg H, Castelli R, Drickamer K, Seeberger PH, Weis WI, 2007, confidence: medium]"},{"id":36,"dataset":"carbohydrate","entity":"Lewis-X trisaccharide (multivalent neoglycoconjugate)","entity_group":"","entity_class":"oligosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"2","unit":"µM","value_reported":"2","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs DC-SIGN for multivalent Lewis-X neoglycoconjugate; reported as Kd < 2 uM","conditions":"Kd vs DC-SIGN for multivalent Lewis-X neoglycoconjugate; reported as Kd < 2 uM","conditions_detail":"Kd vs DC-SIGN for multivalent Lewis-X neoglycoconjugate; reported as Kd < 2 uM | partner: DC-SIGN | technique: binding assay (multivalent)","doi":"10.1016/j.febslet.2006.10.009","source_url":"https://febs.onlinelibrary.wiley.com/doi/10.1016/j.febslet.2006.10.009","year":"2006","confidence":"medium","comments":"\"DC-SIGN binds with Kd < 2 microM to a neoglycoconjugate in which Lewis-X (Lex) trisaccharides are expressed multivalently\"  — Multivalent (avidity) Kd upper bound (<2 uM) for Lewis-X presented multivalently to DC-SIGN.  [van Liempt E, Bank CMC, Mehta P, et al., 2006, confidence: medium]"},{"id":37,"dataset":"carbohydrate","entity":"Man8","entity_group":"","entity_class":"glycan","property":"collision cross section","property_key":"ccs","value":"413","unit":"Å^2","value_reported":"413","unit_reported":"Å^2","method":"Experiment","method_detail":"DTIMS, N2 drift gas, [M+H]+, high-mannose N-glycan","conditions":"DTIMS, N2 drift gas, [M+H]+, high-mannose N-glycan","conditions_detail":"DTIMS, N2 drift gas, [M+H]+, high-mannose N-glycan | adduct: [M+H]+ | drift gas: N2 | ims method: DTIMS","doi":"10.1039/C5AN01092F","source_url":"https://pubs.rsc.org/en/content/articlehtml/2015/an/c5an01092f","year":"2015","confidence":"high","comments":"\"DTCCSN2 (H) 413 Å2\"  — High-mannose N-glycan; N-linked  [Struwe, W.B.; Benesch, J.L.; Harvey, D.J.; Pagel, K., 2015, confidence: high]"},{"id":38,"dataset":"carbohydrate","entity":"Man8","entity_group":"","entity_class":"glycan","property":"collision cross section","property_key":"ccs","value":"415","unit":"Å^2","value_reported":"415","unit_reported":"Å^2","method":"Experiment","method_detail":"DTIMS, N2 drift gas, [M+Na]+, high-mannose N-glycan","conditions":"DTIMS, N2 drift gas, [M+Na]+, high-mannose N-glycan","conditions_detail":"DTIMS, N2 drift gas, [M+Na]+, high-mannose N-glycan | adduct: [M+Na]+ | drift gas: N2 | ims method: DTIMS","doi":"10.1039/C5AN01092F","source_url":"https://pubs.rsc.org/en/content/articlehtml/2015/an/c5an01092f","year":"2015","confidence":"high","comments":"\"DTCCSN2 (Na) 415 Å2\"  — High-mannose N-glycan; N-linked  [Struwe, W.B.; Benesch, J.L.; Harvey, D.J.; Pagel, K., 2015, confidence: high]"},{"id":39,"dataset":"carbohydrate","entity":"Man9","entity_group":"","entity_class":"glycan","property":"collision cross section","property_key":"ccs","value":"436","unit":"Å^2","value_reported":"436","unit_reported":"Å^2","method":"Experiment","method_detail":"DTIMS, N2 drift gas, [M+H]+, high-mannose N-glycan","conditions":"DTIMS, N2 drift gas, [M+H]+, high-mannose N-glycan","conditions_detail":"DTIMS, N2 drift gas, [M+H]+, high-mannose N-glycan | adduct: [M+H]+ | drift gas: N2 | ims method: DTIMS","doi":"10.1039/C5AN01092F","source_url":"https://pubs.rsc.org/en/content/articlehtml/2015/an/c5an01092f","year":"2015","confidence":"high","comments":"\"DTCCSN2 (H) 436 Å2\"  — High-mannose N-glycan; N-linked  [Struwe, W.B.; Benesch, J.L.; Harvey, D.J.; Pagel, K., 2015, confidence: high]"},{"id":40,"dataset":"carbohydrate","entity":"Man9","entity_group":"","entity_class":"glycan","property":"collision cross section","property_key":"ccs","value":"435","unit":"Å^2","value_reported":"435","unit_reported":"Å^2","method":"Experiment","method_detail":"DTIMS, N2 drift gas, [M+Na]+, high-mannose N-glycan","conditions":"DTIMS, N2 drift gas, [M+Na]+, high-mannose N-glycan","conditions_detail":"DTIMS, N2 drift gas, [M+Na]+, high-mannose N-glycan | adduct: [M+Na]+ | drift gas: N2 | ims method: DTIMS","doi":"10.1039/C5AN01092F","source_url":"https://pubs.rsc.org/en/content/articlehtml/2015/an/c5an01092f","year":"2015","confidence":"high","comments":"\"DTCCSN2 (Na) 435 Å2\"  — High-mannose N-glycan; N-linked  [Struwe, W.B.; Benesch, J.L.; Harvey, D.J.; Pagel, K., 2015, confidence: high]"}]}