BMRB Entry 11573
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11573
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of the human BMX SH2 domain PubMed: 26293126
Deposition date: 2014-07-31 Original release date: 2018-12-11
Authors: Kasai, Takuma; Koshiba, Seizo; Watanabe, Satoru; Harada, Takushi; Kigawa, Takanori; Yokoyama, Shigeyuki
Citation: Kasai, Takuma; Koshiba, Seizo; Yokoyama, Jun; Kigawa, Takanori. "Stable isotope labeling strategy based on coding theory." J. Biomol. NMR 63, 213-221 (2015).
Assembly members:
BMX_SH2_domain, polymer, 110 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: cell free synthesis Host organism: E. coli - cell free Vector: P061225-65
Entity Sequences (FASTA):
BMX_SH2_domain: GSSGSSGLDDYDWFAGNISR
SQSEQLLRQKGKEGAFMVRN
SSQVGMYTVSLFSKAVNDKK
GTVKHYHVHTNAENKLYLAE
NYCFDSIPKLIHYHQHNSAG
MITRLRHPVS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 468 |
15N chemical shifts | 116 |
1H chemical shifts | 739 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | BMX SH2 domain | 1 |
Entities:
Entity 1, BMX SH2 domain 110 residues - Formula weight is not available
Residues 1-7 represent a non-native cloning artifact. This is the SH2 domain of human BMX protein.
1 | GLY | SER | SER | GLY | SER | SER | GLY | LEU | ASP | ASP | |
2 | TYR | ASP | TRP | PHE | ALA | GLY | ASN | ILE | SER | ARG | |
3 | SER | GLN | SER | GLU | GLN | LEU | LEU | ARG | GLN | LYS | |
4 | GLY | LYS | GLU | GLY | ALA | PHE | MET | VAL | ARG | ASN | |
5 | SER | SER | GLN | VAL | GLY | MET | TYR | THR | VAL | SER | |
6 | LEU | PHE | SER | LYS | ALA | VAL | ASN | ASP | LYS | LYS | |
7 | GLY | THR | VAL | LYS | HIS | TYR | HIS | VAL | HIS | THR | |
8 | ASN | ALA | GLU | ASN | LYS | LEU | TYR | LEU | ALA | GLU | |
9 | ASN | TYR | CYS | PHE | ASP | SER | ILE | PRO | LYS | LEU | |
10 | ILE | HIS | TYR | HIS | GLN | HIS | ASN | SER | ALA | GLY | |
11 | MET | ILE | THR | ARG | LEU | ARG | HIS | PRO | VAL | SER |
Samples:
sample_1: BMX SH2 domain, [U-13C; U-15N], 1.13 mM; Tris-Cl, [U-2H], 20 mM; sodium chloride 100 mM; DTT, [U-2H], 1 mM; sodium azide 0.02 % (w/v); H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr v3.5, Bruker Biospin - collection
NMRPipe v20031121, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5.0.4, Johnson, One Moon Scientific - data analysis, peak picking
Kujira v0.9810, Naohiro Kobayashi - chemical shift assignment, data analysis, peak picking
CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- 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