BMRB Entry 30389
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30389
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Title: Solution structure of AGL55
Deposition date: 2017-12-24 Original release date: 2019-01-11
Authors: Qiu, C.; Yuan, Y.; Castellino, F.
Citation: Qiu, C.; Yuan, Y.; Zajicek, J.; Ploplis, V.; Lee, S.; Castellino, F.. "The C-Domain Repeats in Plasminogen-binding Group A Streptococcal M-Protein are Essential Determinants for its Dimerization" . ., .-..
Assembly members:
entity_1, polymer, 57 residues, 6742.396 Da.
Natural source: Common Name: Streptococcus pyogenes Taxonomy ID: 1138874 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: GSAGLQEKERELEDLKDAEL
KRLNEERHDHDKREAERKAL
EDKLADKQEHLDGALRY
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 236 |
| 15N chemical shifts | 54 |
| 1H chemical shifts | 363 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 57 residues - 6742.396 Da.
| 1 | GLY | SER | ALA | GLY | LEU | GLN | GLU | LYS | GLU | ARG | ||||
| 2 | GLU | LEU | GLU | ASP | LEU | LYS | ASP | ALA | GLU | LEU | ||||
| 3 | LYS | ARG | LEU | ASN | GLU | GLU | ARG | HIS | ASP | HIS | ||||
| 4 | ASP | LYS | ARG | GLU | ALA | GLU | ARG | LYS | ALA | LEU | ||||
| 5 | GLU | ASP | LYS | LEU | ALA | ASP | LYS | GLN | GLU | HIS | ||||
| 6 | LEU | ASP | GLY | ALA | LEU | ARG | TYR |
Samples:
sample_1: BisTris-d19, [U-99% 2H], 20 mM; DSS 1 mM; sodium azide 1 mM; EDTA 1 mM
sample_conditions_1: ionic strength: 20 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, data analysis, processing
SPARKY, Goddard - chemical shift assignment, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - 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