BMRB Entry 30600
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30600
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of truncated peptide from PAMap53
Deposition date: 2019-04-15 Original release date: 2020-02-21
Authors: Yuan, Y.; Castellino, F.
Citation: Yuan, Y.; Ploplis, V.; Lee, S.; Castellino, F.. "Solution structural model of the complex of the binding regions of human plasminogen with its M-protein receptor from Streptococcal pyogenes cells" . ., .-..
Assembly members:
entity_1, polymer, 52 residues, 6020.605 Da.
Natural source: Common Name: Streptococcus pyogenes Taxonomy ID: 1314 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pyogenes
Experimental source: Production method: recombinant technology Host organism: Escherichia coli DH5[alpha]
Entity Sequences (FASTA):
entity_1: GSVEKLTADAELQRLKNERH
EEAELERLKSEAADHDKKEA
ERKALEDKLADY
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 198 |
| 15N chemical shifts | 50 |
| 1H chemical shifts | 313 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 52 residues - 6020.605 Da.
| 1 | GLY | SER | VAL | GLU | LYS | LEU | THR | ALA | ASP | ALA | ||||
| 2 | GLU | LEU | GLN | ARG | LEU | LYS | ASN | GLU | ARG | HIS | ||||
| 3 | GLU | GLU | ALA | GLU | LEU | GLU | ARG | LEU | LYS | SER | ||||
| 4 | GLU | ALA | ALA | ASP | HIS | ASP | LYS | LYS | GLU | ALA | ||||
| 5 | GLU | ARG | LYS | ALA | LEU | GLU | ASP | LYS | LEU | ALA | ||||
| 6 | ASP | TYR |
Samples:
sample_1: Truncated peptide from PAMAP53, [U-99% 13C; U-99% 15N], 0.5 mM; Bis-Tris-d19, [U-2H], 20 mM; DSS 2 ug/mL; sodium azide 1 ug/mL
sample_conditions_1: ionic strength: 20 mM; 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 |
| 2D NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin v3.5, Bruker Biospin - collection
Sparky, Goddard - chemical shift assignment, data analysis
CS-ROSETTA, Shen, Vernon, Baker and Bax - structure calculation
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMR spectrometers:
- Bruker AvanceII 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts