BMRB Entry 26972
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26972
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
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Citation: Li, Yan; Ng, Hui Qi; Ngo, Anna; Liu, Shuang; Tan, Yih Wan; Kwek, Perlyn Zekui; Hung, Alvin; Joy, Joma; Hill, Jeffrey; Keller, Thomas; Kang, CongBao. "Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor" Biomol. NMR Assign. 11, 225-229 (2017).
PubMed: 28808922
Assembly members:
SET_domain_of_human_methyltransferase_NSD3, polymer, 258 residues, Formula weight is not available
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: pET29b
Entity Sequences (FASTA):
SET_domain_of_human_methyltransferase_NSD3: MQELKAQRESKEALEIEKNS
RKPPPYKHIKANKVIGKVQI
QVADLSEIPRCNCKPADENP
CGLESECLNRMLQYECHPQV
CPAGDRCQNQCFTKRLYPDA
EIIKTERRGWGLRTKRSIKK
GEFVNEYVGELIDEEECRLR
IKRAHENSVTNFYMLTVTKD
RIIDAGPKGNYSRFMNHSCN
PNCETQKWTVNGDVRVGLFA
LCDIPAGMELTFNYNLDCLG
NGRTECHCGADNCSGFLGVR
PKSACASTNEEKHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 691 |
| 15N chemical shifts | 224 |
| 1H chemical shifts | 224 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SET domain of human methyltransferase NSD3 | 1 |
Entities:
Entity 1, SET domain of human methyltransferase NSD3 258 residues - Formula weight is not available
| 1 | MET | GLN | GLU | LEU | LYS | ALA | GLN | ARG | GLU | SER | ||||
| 2 | LYS | GLU | ALA | LEU | GLU | ILE | GLU | LYS | ASN | SER | ||||
| 3 | ARG | LYS | PRO | PRO | PRO | TYR | LYS | HIS | ILE | LYS | ||||
| 4 | ALA | ASN | LYS | VAL | ILE | GLY | LYS | VAL | GLN | ILE | ||||
| 5 | GLN | VAL | ALA | ASP | LEU | SER | GLU | ILE | PRO | ARG | ||||
| 6 | CYS | ASN | CYS | LYS | PRO | ALA | ASP | GLU | ASN | PRO | ||||
| 7 | CYS | GLY | LEU | GLU | SER | GLU | CYS | LEU | ASN | ARG | ||||
| 8 | MET | LEU | GLN | TYR | GLU | CYS | HIS | PRO | GLN | VAL | ||||
| 9 | CYS | PRO | ALA | GLY | ASP | ARG | CYS | GLN | ASN | GLN | ||||
| 10 | CYS | PHE | THR | LYS | ARG | LEU | TYR | PRO | ASP | ALA | ||||
| 11 | GLU | ILE | ILE | LYS | THR | GLU | ARG | ARG | GLY | TRP | ||||
| 12 | GLY | LEU | ARG | THR | LYS | ARG | SER | ILE | LYS | LYS | ||||
| 13 | GLY | GLU | PHE | VAL | ASN | GLU | TYR | VAL | GLY | GLU | ||||
| 14 | LEU | ILE | ASP | GLU | GLU | GLU | CYS | ARG | LEU | ARG | ||||
| 15 | ILE | LYS | ARG | ALA | HIS | GLU | ASN | SER | VAL | THR | ||||
| 16 | ASN | PHE | TYR | MET | LEU | THR | VAL | THR | LYS | ASP | ||||
| 17 | ARG | ILE | ILE | ASP | ALA | GLY | PRO | LYS | GLY | ASN | ||||
| 18 | TYR | SER | ARG | PHE | MET | ASN | HIS | SER | CYS | ASN | ||||
| 19 | PRO | ASN | CYS | GLU | THR | GLN | LYS | TRP | THR | VAL | ||||
| 20 | ASN | GLY | ASP | VAL | ARG | VAL | GLY | LEU | PHE | ALA | ||||
| 21 | LEU | CYS | ASP | ILE | PRO | ALA | GLY | MET | GLU | LEU | ||||
| 22 | THR | PHE | ASN | TYR | ASN | LEU | ASP | CYS | LEU | GLY | ||||
| 23 | ASN | GLY | ARG | THR | GLU | CYS | HIS | CYS | GLY | ALA | ||||
| 24 | ASP | ASN | CYS | SER | GLY | PHE | LEU | GLY | VAL | ARG | ||||
| 25 | PRO | LYS | SER | ALA | CYS | ALA | SER | THR | ASN | GLU | ||||
| 26 | GLU | LYS | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: SET domain of human methyltransferase NSD3, [U-13C; U-15N; U-2H], 0.5 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM
sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Keller and Wuthrich - chemical shift assignment, processing
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks