BMRB Entry 27415
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27415
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Title: Chemical shift assignments for TRAP, a MMP20 proteolysis product of murine amelogenin. PubMed: 29960917
Deposition date: 2018-03-05 Original release date: 2018-04-11
Authors: Buchko, Garry
Citation: Buchko, Garry; Jayasinha Arachchige, Rajith; Tao, Jinhui; Tarasevich, Barbara; Shaw, Wendy. "Identification of major matrix metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amelogenin peptide using a nuclear magnetic resonance spectroscopy based method" Arch. Oral Biol. 93, 187-194 (2018).
Assembly members:
TRAP, polymer, 49 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pJexpress414
Entity Sequences (FASTA):
TRAP: GPGSMPLPPHPGSPGYINLS
YEVLTPLKWYQSMIRQPYPS
YGYEPMGGW
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 162 |
15N chemical shifts | 42 |
1H chemical shifts | 150 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | TRAP | 1 |
Entities:
Entity 1, TRAP 49 residues - Formula weight is not available
1 | GLY | PRO | GLY | SER | MET | PRO | LEU | PRO | PRO | HIS | ||||
2 | PRO | GLY | SER | PRO | GLY | TYR | ILE | ASN | LEU | SER | ||||
3 | TYR | GLU | VAL | LEU | THR | PRO | LEU | LYS | TRP | TYR | ||||
4 | GLN | SER | MET | ILE | ARG | GLN | PRO | TYR | PRO | SER | ||||
5 | TYR | GLY | TYR | GLU | PRO | MET | GLY | GLY | TRP |
Samples:
sample_1: TRAP, [U-99% 13C; U-99% 15N], 0.5 mM; acetic acid 2%
sample_conditions_1: ionic strength: 0 M; pH: 2.8; pressure: 1 atm; temperature: 273 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
Felix v2007, Accelrys Software Inc. - processing
SPARKY v1.4, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 750 MHz
- Agilent VXRS 600 MHz
- Agilent VXRS 750 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts