BMRB Entry 26721
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26721
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Title: RXFP1-LDLa linker PubMed: 26612092
Deposition date: 2015-12-13 Original release date: 2016-02-12
Authors: Sethi, Ashish; Gooley, Paul
Citation: Tailhades, J.; Sethi, Ashish; Petrie, Emma; Gooley, Paul; Bathgate, Ross; Wade, R.; Hossain, Mohammed. "Native Chemical Ligation to Minimize Aspartimide Formation during Chemical Synthesis of Small LDLa Protein" Chemistry 22, 1146-1151 (2016).
Assembly members:
RXFP1(1-72), polymer, 72 residues, 8128.9 Da.
entity_CA, non-polymer, 40.078 Da.
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
Entity Sequences (FASTA):
RXFP1(1-72): QDVKCSLGYFPCGNITKCLP
QLLHCNGVDDCGNQADEDNC
GDNNGWSLQFDKYFASYYKM
TSQYPFEAETPE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 198 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 132 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RXFP1(1-72) | 1 |
| 2 | Calcium | 2 |
Entities:
Entity 1, RXFP1(1-72) 72 residues - 8128.9 Da.
| 1 | GLN | ASP | VAL | LYS | CYS | SER | LEU | GLY | TYR | PHE | ||||
| 2 | PRO | CYS | GLY | ASN | ILE | THR | LYS | CYS | LEU | PRO | ||||
| 3 | GLN | LEU | LEU | HIS | CYS | ASN | GLY | VAL | ASP | ASP | ||||
| 4 | CYS | GLY | ASN | GLN | ALA | ASP | GLU | ASP | ASN | CYS | ||||
| 5 | GLY | ASP | ASN | ASN | GLY | TRP | SER | LEU | GLN | PHE | ||||
| 6 | ASP | LYS | TYR | PHE | ALA | SER | TYR | TYR | LYS | MET | ||||
| 7 | THR | SER | GLN | TYR | PRO | PHE | GLU | ALA | GLU | THR | ||||
| 8 | PRO | GLU |
Entity 2, Calcium - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_1: RXFP1(1-72), [U-100% 13C; U-100% 15N; U-80% 2H], 100 uM; calcium 10 mM; imidazole 50 mM
sample_2: RXFP1(1-72), [U-100% 13C; U-100% 15N], 100 uM; calcium 10 mM; imidazole 50 mM
sample_conditions_1: ionic strength: 0 M; pH: 6.8; pressure: 1 atm; temperature: 298 K
sample_conditions_2: pH: 6.8; 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)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D HNHA | sample_2 | isotropic | sample_conditions_2 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
TOPSPIN, Bruker Biospin - collection
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