BMRB Entry 30390
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30390
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of KTI55 PubMed: 30071314
Deposition date: 2017-12-24 Original release date: 2019-01-11
Authors: Castellino, F.; Qiu, C.; Yuan, Y.
Citation: Qiu, Cunjia; Yuan, Yue; Zajicek, Jaroslav; Liang, Zhong; Balsara, Rashna; Brito-Robionson, Teresa; Lee, Shaun; Ploplis, Victoria; Castellino, Francis. "Contributions of different modules of the plasminogen-binding Streptococcus pyogenes M-protein that mediate its functional dimerization" J. Struct. Biol. 204, 151-164 (2018).
Assembly members:
entity_1, polymer, 57 residues, 6799.461 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] Vector: pET15b
Entity Sequences (FASTA):
entity_1: GSKTIQEKEQELKNLKDNVE
LERLKNERHDHDEEAERKAL
EDKLADKQEHLDGALRY
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 239 |
| 15N chemical shifts | 55 |
| 1H chemical shifts | 354 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 57 residues - 6799.461 Da.
| 1 | GLY | SER | LYS | THR | ILE | GLN | GLU | LYS | GLU | GLN | ||||
| 2 | GLU | LEU | LYS | ASN | LEU | LYS | ASP | ASN | VAL | GLU | ||||
| 3 | LEU | GLU | ARG | LEU | LYS | ASN | GLU | ARG | HIS | ASP | ||||
| 4 | HIS | ASP | GLU | 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 HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts