BMRB Entry 50283
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50283
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Title: Backbone and methyl chemical shift assignments, relaxation data and order parameters of Galectin-3C in complex with meta-fluoroaryltriazole galactopyranosyl 1-thio-D-glucopyranoside derivative
Deposition date: 2020-05-20 Original release date: 2020-12-02
Authors: Wallerstein, Johan; Misini Ignjatovic, Majda; Kumar, Rohit; Caldararu, Octav; Peterson, Kristoffer; Leffler, Hakon; Logan, Derek; Nilsson, Ulf; Ryde, Ulf; Akke, Mikael
Citation: Wallerstein, Johan; Ekberg, Vilhelm; Misini Ignjatovic, Majda; Kumar, Rohit; Caldararu, Octav; Peterson, Kristoffer; Wernersson, Sven; Brath, Ulrika; Leffler, Hakon; Oksanen, Esko; Logan, Derek; Nilsson, Ulf; Ryde, Ulf; Akke, Mikael. "Entropy-Entropy Compensation between the Protein, Ligand, and Solvent Degrees of Freedom Fine-Tunes Affinity in Ligand Binding to Galectin-3C" JACS Au. 1, 484-500 (2021).
Assembly members:
entity_1, polymer, . residues, Formula weight is not available
entity_KOW, non-polymer, 503.499 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pLysS pGal3CRD
Entity Sequences (FASTA):
entity_1: PLIVPYNLPLPGGVVPRMLI
TILGTVKPNANRIALDFQRG
NDVAFHFNPRFNENNRRVIV
CNTKLDNNWGREERQSVFPF
ESGKPFKIQVLVEPDHFKVA
VNDAHLLQYNHRVKKLNEIS
KLGISGDIDLTSASYTMI
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- order_parameters
| Data type | Count |
| 13C chemical shifts | 85 |
| 15N chemical shifts | 122 |
| 1H chemical shifts | 377 |
| T1 relaxation values | 365 |
| T2 relaxation values | 365 |
| heteronuclear NOE values | 365 |
| order parameters | 189 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | gal3C | 1 |
| 2 | ligand M | 2 |
Entities:
Entity 1, gal3C - Formula weight is not available
| 1 | PRO | LEU | ILE | VAL | PRO | TYR | ASN | LEU | PRO | LEU | ||||
| 2 | PRO | GLY | GLY | VAL | VAL | PRO | ARG | MET | LEU | ILE | ||||
| 3 | THR | ILE | LEU | GLY | THR | VAL | LYS | PRO | ASN | ALA | ||||
| 4 | ASN | ARG | ILE | ALA | LEU | ASP | PHE | GLN | ARG | GLY | ||||
| 5 | ASN | ASP | VAL | ALA | PHE | HIS | PHE | ASN | PRO | ARG | ||||
| 6 | PHE | ASN | GLU | ASN | ASN | ARG | ARG | VAL | ILE | VAL | ||||
| 7 | CYS | ASN | THR | LYS | LEU | ASP | ASN | ASN | TRP | GLY | ||||
| 8 | ARG | GLU | GLU | ARG | GLN | SER | VAL | PHE | PRO | PHE | ||||
| 9 | GLU | SER | GLY | LYS | PRO | PHE | LYS | ILE | GLN | VAL | ||||
| 10 | LEU | VAL | GLU | PRO | ASP | HIS | PHE | LYS | VAL | ALA | ||||
| 11 | VAL | ASN | ASP | ALA | HIS | LEU | LEU | GLN | TYR | ASN | ||||
| 12 | HIS | ARG | VAL | LYS | LYS | LEU | ASN | GLU | ILE | SER | ||||
| 13 | LYS | LEU | GLY | ILE | SER | GLY | ASP | ILE | ASP | LEU | ||||
| 14 | THR | SER | ALA | SER | TYR | THR | MET | ILE |
Entity 2, ligand M - C20 H26 F N3 O9 S - 503.499 Da.
| 1 | KOW |
Samples:
sample_1: Galectin-3C, [U-100% 15N], 0.85 mM; ligand M 0.32 ± 0.02 mM; HEPES 5 mM; D2O, [U-2H], 10%
sample_2: Galectin-3C, [U-100% 13C; U-100% 15N], 0.85 mM; ligand M 0.32 ± 0.02 mM; HEPES 5 mM; D2O, [U-2H], 10%
sample_3: Galectin-3C, [U-100% 13C; U-100% 15N; U-60% 2H], 0.85 mM; ligand M 0.32 ± 0.02 mM; HEPES 5 mM; D2O, [U-2H], 10%
sample_conditions_1: pH: 7.4; temperature: 301 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| T1/R1 relaxation 500 | sample_1 | isotropic | sample_conditions_1 |
| T1/R1 relaxation 600 | sample_1 | isotropic | sample_conditions_1 |
| T1/R1 relaxation 800 | sample_1 | isotropic | sample_conditions_1 |
| T2/R2 relaxation 500 | sample_1 | isotropic | sample_conditions_1 |
| T2/R2 relaxation 600 | sample_1 | isotropic | sample_conditions_1 |
| T2/R2 relaxation 800 | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe 500 | sample_1 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe 600 | sample_1 | isotropic | sample_conditions_1 |
| 1H-15N heteronoe 800 | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| R1(Dz)_methyl 500 | sample_3 | isotropic | sample_conditions_1 |
| R1(Dz)_methyl 600 | sample_3 | isotropic | sample_conditions_1 |
| R2(D+)_methyl 500 | sample_3 | isotropic | sample_conditions_1 |
| R2(D+)_methyl 600 | sample_3 | isotropic | sample_conditions_1 |
| R(3Dz^2-2)_methyl 500 | sample_3 | isotropic | sample_conditions_1 |
| R(3Dz^2-2)_methyl 600 | sample_3 | isotropic | sample_conditions_1 |
| R(D+Dz + DzD+)_methyl 500 | sample_3 | isotropic | sample_conditions_1 |
| R(D+Dz + DzD+)_methyl 600 | sample_3 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
Software:
CcpNmr Analysis v2.0 - chemical shift assignment, data analysis, peak picking
Chimera v1.13 - data analysis, geometry optimization
NMRPipe - data analysis, processing
NMRDraw - data analysis
PiNT v2.1.0 - chemical shift calculation, peak picking
Relax v4.0.320 - data analysis, refinement
Matlab v2018b - data analysis, model-free fitting
NMR spectrometers:
- Varian VNMRS 500 MHz
- Varian VNMRS 600 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts