BMRB Entry 17477
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17477
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Title: NMR Structure of the Mouse MFG-E8 C2 Domain PubMed: 23262193
Deposition date: 2011-02-21 Original release date: 2012-08-31
Authors: Ye, Hong; Subramanian, Vivekanandan; Yu, Liang; Yoon, Ho Sup
Citation: Ye, Hong; Li, Baihong; Subramanian, Vivekanandan; Choi, Bo-Hwa; Yu, Liang; Harikishore, Amaravadhi; Harikishore, Amaravadhi; Chakraborty, Goutam; Baek, Kwanghee; Yoon, Ho Sup. "NMR solution structure of C2 domain of MFG-E8 and insights into its molecular recognition with phosphatidylserine" Biochim. Biophys. Acta 1828, 1083-1093 (2013).
Assembly members:
MFG-E8_C2_domain, polymer, 170 residues, 18609.027 Da.
Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MFG-E8_C2_domain: MKSGHGCSEPLGLKNNTIPD
SQMSASSSYKTWNLRAFGWY
PHLGRLDNQGKINAWTAQSN
SAKEWLQVDLGTQRQVTGII
TQGARDFGHIQYVASYKVAH
SDDGVQWTVYEEQGSSKVFQ
GNLDNNSHKKNIFEKPFMAR
YVRVLPVSWHNRITLRLELL
GCLEHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 573 |
15N chemical shifts | 160 |
1H chemical shifts | 973 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MFG-E8_C2_domain | 1 |
Entities:
Entity 1, MFG-E8_C2_domain 170 residues - 18609.027 Da.
1 | MET | LYS | SER | GLY | HIS | GLY | CYS | SER | GLU | PRO | |
2 | LEU | GLY | LEU | LYS | ASN | ASN | THR | ILE | PRO | ASP | |
3 | SER | GLN | MET | SER | ALA | SER | SER | SER | TYR | LYS | |
4 | THR | TRP | ASN | LEU | ARG | ALA | PHE | GLY | TRP | TYR | |
5 | PRO | HIS | LEU | GLY | ARG | LEU | ASP | ASN | GLN | GLY | |
6 | LYS | ILE | ASN | ALA | TRP | THR | ALA | GLN | SER | ASN | |
7 | SER | ALA | LYS | GLU | TRP | LEU | GLN | VAL | ASP | LEU | |
8 | GLY | THR | GLN | ARG | GLN | VAL | THR | GLY | ILE | ILE | |
9 | THR | GLN | GLY | ALA | ARG | ASP | PHE | GLY | HIS | ILE | |
10 | GLN | TYR | VAL | ALA | SER | TYR | LYS | VAL | ALA | HIS | |
11 | SER | ASP | ASP | GLY | VAL | GLN | TRP | THR | VAL | TYR | |
12 | GLU | GLU | GLN | GLY | SER | SER | LYS | VAL | PHE | GLN | |
13 | GLY | ASN | LEU | ASP | ASN | ASN | SER | HIS | LYS | LYS | |
14 | ASN | ILE | PHE | GLU | LYS | PRO | PHE | MET | ALA | ARG | |
15 | TYR | VAL | ARG | VAL | LEU | PRO | VAL | SER | TRP | HIS | |
16 | ASN | ARG | ILE | THR | LEU | ARG | LEU | GLU | LEU | LEU | |
17 | GLY | CYS | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: sodium phosphate 20 mM; sodium chloride 20 mM; sodium azide 0.01%; MFG-E8 C2 domain, [U-13C; U-15N], 0.8 mM; H2O 90%; D2O 10%
sample_2: sodium phosphate 20 mM; sodium chloride 20 mM; sodium azide 0.01%; MFG-E8 C2 domain, [U-13C; U-15N], 0.8 mM; D2O 100%
sample_conditions_1: ionic strength: 0.02 M; 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D H(CC)(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D (H)CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts