BMRB Entry 27584
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27584
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Title: Backbone 1H, 15N, 13C chemical shift assignments for the MAK33 CH2 antibody domain PubMed: 30228183
Deposition date: 2018-08-23 Original release date: 2018-09-18
Authors: Weber, Benedikt; Berner, Carolin; Feind, Gina; Buchner, Johannes; Brandl, Matthias; Pradhan, Tejaswini; Reif, Bernd; Pulido Cendales, Maria Daniela; Zacharias, Martin
Citation: Weber, Benedikt; Brandl, Matthias; Pulido Cendales, Maria Daniela; Berner, Carolin; Pradhan, Tejaswini; Feind, Gina Maria; Zacharias, Martin; Reif, Bernd; Buchner, Johannes. "A single residue switch reveals principles of antibody domain integrity." J. Biol. Chem. 293, 17107-17118 (2018).
Assembly members:
CH2, polymer, 99 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b
Entity Sequences (FASTA):
CH2: SSVFIFPPKPKDVLTITLTP
KVTCVVVDISKDDPEVQFSW
FVDDVEVHTAQTQPREEQFN
STFRSVSELPIMHQDWLNGK
EFKCRVNSAAFPAPIEKTI
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 152 |
15N chemical shifts | 66 |
1H chemical shifts | 66 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | CH2 wild type | 1 |
Entities:
Entity 1, CH2 wild type 99 residues - Formula weight is not available
CH2 domain wild type without any N- or C-terminal extensions.
1 | SER | SER | VAL | PHE | ILE | PHE | PRO | PRO | LYS | PRO | ||||
2 | LYS | ASP | VAL | LEU | THR | ILE | THR | LEU | THR | PRO | ||||
3 | LYS | VAL | THR | CYS | VAL | VAL | VAL | ASP | ILE | SER | ||||
4 | LYS | ASP | ASP | PRO | GLU | VAL | GLN | PHE | SER | TRP | ||||
5 | PHE | VAL | ASP | ASP | VAL | GLU | VAL | HIS | THR | ALA | ||||
6 | GLN | THR | GLN | PRO | ARG | GLU | GLU | GLN | PHE | ASN | ||||
7 | SER | THR | PHE | ARG | SER | VAL | SER | GLU | LEU | PRO | ||||
8 | ILE | MET | HIS | GLN | ASP | TRP | LEU | ASN | GLY | LYS | ||||
9 | GLU | PHE | LYS | CYS | ARG | VAL | ASN | SER | ALA | ALA | ||||
10 | PHE | PRO | ALA | PRO | ILE | GLU | LYS | THR | ILE |
Samples:
sample_1: CH2, [U-98% 13C; U-98% 15N], 550 uM; sodium phosphate 9.1 mM; potassium phosphate 1.6 mM; sodium chloride 125 mM; potassium chloride 2.5 mM
sample_conditions_1: ionic strength: 148 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CCPNMR_Analysis v2.4.2, CCPN - chemical shift assignment, peak picking
TOPSPIN v4.0.1, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts