Glyco Property List
Pooled literature properties (glycanDB). Optional filters: ?dataset=uv_vis&property_key=...
GET /api/gdd/glyco-properties/?format=api&page=2
{ "count": 839, "next": "http://glycodata.org/api/gdd/glyco-properties/?format=api&page=3", "previous": "http://glycodata.org/api/gdd/glyco-properties/?format=api", "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]" } ] }