BMRB Entry 52417
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52417
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Title: B2_3
Deposition date: 2024-04-19 Original release date: 2024-06-26
Authors: Bi, Yunchen; Wu, Yujie
Citation: Liu, Yuxin; Wu, Yujie; Bi, Yunchen. "1H, 13C and 15N resonance assignments of a variable domain of shark new antigen receptor against hyaluronan synthase" Biomol. NMR Assignments ., .-..
Assembly members:
entity_1, polymer, 110 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b
Entity Sequences (FASTA):
entity_1: MAERVEQTPTTTTKEAGESL
TVNCVLKGSSCALGNTYWYF
TKKGATKKASLSTGGRYSDT
KNTASKSFSLRISDLRVEDS
GTYHCEAYTCAGGTPWRHYI
EGGGTILTVK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 356 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 474 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | A type of single domain antibody | 1 |
Entities:
Entity 1, A type of single domain antibody 110 residues - Formula weight is not available
| 1 | MET | ALA | GLU | ARG | VAL | GLU | GLN | THR | PRO | THR | |
| 2 | THR | THR | THR | LYS | GLU | ALA | GLY | GLU | SER | LEU | |
| 3 | THR | VAL | ASN | CYS | VAL | LEU | LYS | GLY | SER | SER | |
| 4 | CYS | ALA | LEU | GLY | ASN | THR | TYR | TRP | TYR | PHE | |
| 5 | THR | LYS | LYS | GLY | ALA | THR | LYS | LYS | ALA | SER | |
| 6 | LEU | SER | THR | GLY | GLY | ARG | TYR | SER | ASP | THR | |
| 7 | LYS | ASN | THR | ALA | SER | LYS | SER | PHE | SER | LEU | |
| 8 | ARG | ILE | SER | ASP | LEU | ARG | VAL | GLU | ASP | SER | |
| 9 | GLY | THR | TYR | HIS | CYS | GLU | ALA | TYR | THR | CYS | |
| 10 | ALA | GLY | GLY | THR | PRO | TRP | ARG | HIS | TYR | ILE | |
| 11 | GLU | GLY | GLY | GLY | THR | ILE | LEU | THR | VAL | LYS |
Samples:
sample_1: A type of single domain antibody, [U-100% 13C; U-100% 15N], 0.5 mM; D2O, [U-100% 2H], 10%; H2O 90%; sodium phosphate 50 mM
sample_conditions_1: ionic strength: 0.3 M; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
NMR spectrometers:
- Bruker AVANCE NEO 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts