BMRB Entry 17549
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17549
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Title: Backbone Resonance Assignment of the von-Willebrand-factor-A-like domain 2 of type VII collagen PubMed: 21570975
Deposition date: 2011-03-24 Original release date: 2011-05-04
Authors: Leineweber, Sarah
Citation: Leineweber, Sarah; Schonig, Sarah; Seeger, Karsten. "Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR." FEBS Lett. 585, 1748-1752 (2011).
Assembly members:
mvWFA2, polymer, 196 residues, Formula weight is not available
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):
mvWFA2: GRAMGACSHGPVDVVFLLHA
TRDNAHNAEAVRRVLERLVS
ALGPLGPQAAQVGLLTYSHR
PSPLFPLNSSHDLGIILRKI
RDIPYVDPSGNNLGTAVTTA
HRYLLASNAPGRRQQVPGVM
VLLVDEPLRGDILSPIREAQ
TSGLKVMALSLVGADPEQLR
RLAPGTDPIQNFFAVDNGPG
LDRAVSDLAVALCQAA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 325 |
15N chemical shifts | 167 |
1H chemical shifts | 366 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | mvWFA2 | 1 |
Entities:
Entity 1, mvWFA2 196 residues - Formula weight is not available
1 | GLY | ARG | ALA | MET | GLY | ALA | CYS | SER | HIS | GLY | ||||
2 | PRO | VAL | ASP | VAL | VAL | PHE | LEU | LEU | HIS | ALA | ||||
3 | THR | ARG | ASP | ASN | ALA | HIS | ASN | ALA | GLU | ALA | ||||
4 | VAL | ARG | ARG | VAL | LEU | GLU | ARG | LEU | VAL | SER | ||||
5 | ALA | LEU | GLY | PRO | LEU | GLY | PRO | GLN | ALA | ALA | ||||
6 | GLN | VAL | GLY | LEU | LEU | THR | TYR | SER | HIS | ARG | ||||
7 | PRO | SER | PRO | LEU | PHE | PRO | LEU | ASN | SER | SER | ||||
8 | HIS | ASP | LEU | GLY | ILE | ILE | LEU | ARG | LYS | ILE | ||||
9 | ARG | ASP | ILE | PRO | TYR | VAL | ASP | PRO | SER | GLY | ||||
10 | ASN | ASN | LEU | GLY | THR | ALA | VAL | THR | THR | ALA | ||||
11 | HIS | ARG | TYR | LEU | LEU | ALA | SER | ASN | ALA | PRO | ||||
12 | GLY | ARG | ARG | GLN | GLN | VAL | PRO | GLY | VAL | MET | ||||
13 | VAL | LEU | LEU | VAL | ASP | GLU | PRO | LEU | ARG | GLY | ||||
14 | ASP | ILE | LEU | SER | PRO | ILE | ARG | GLU | ALA | GLN | ||||
15 | THR | SER | GLY | LEU | LYS | VAL | MET | ALA | LEU | SER | ||||
16 | LEU | VAL | GLY | ALA | ASP | PRO | GLU | GLN | LEU | ARG | ||||
17 | ARG | LEU | ALA | PRO | GLY | THR | ASP | PRO | ILE | GLN | ||||
18 | ASN | PHE | PHE | ALA | VAL | ASP | ASN | GLY | PRO | GLY | ||||
19 | LEU | ASP | ARG | ALA | VAL | SER | ASP | LEU | ALA | VAL | ||||
20 | ALA | LEU | CYS | GLN | ALA | ALA |
Samples:
sample_1: mvWFA2, [U-100% 13C; U-100% 15N], 2 mM; potassium phosphate 10 mM; TSP 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0 M; 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 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker DRX 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts