BMRB Entry 27550
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27550
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Macdonald, Ramsay; Cascio, Duilio; Collazo, Michael; Phillips, Martin; Clubb, Robert. "The Streptococcus pyogenes Shr protein captures human hemoglobin using two structurally unique binding domains" J. Biol. Chem. 293, 18365-18377 (2018).
PubMed: 30301765
Assembly members:
Shr-HID2, polymer, 132 residues, Formula weight is not available
Natural source: Common Name: Streptococcus pyogenes Taxonomy ID: 1314 Superkingdom: not available Kingdom: not available Genus/species: Streptococcus pyogenes
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pRAM402
Entity Sequences (FASTA):
Shr-HID2: SKTVPQNQGTQKVVKSGKNT
ANLSLITKLSQEDGAILFPE
IDRYSDNKQIKALTQQITKV
TVNGTVYKDLISDSVKDTNG
WVSNMTGLHLGTKAFKDGEN
TIVISSKGFEDVTITVTKKD
GQIHFVSAKQKQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 357 |
| 15N chemical shifts | 123 |
| 1H chemical shifts | 441 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Shr-HID2 | 1 |
Entities:
Entity 1, Shr-HID2 132 residues - Formula weight is not available
The first serine residue is a cloning artifact.
| 1 | SER | LYS | THR | VAL | PRO | GLN | ASN | GLN | GLY | THR | ||||
| 2 | GLN | LYS | VAL | VAL | LYS | SER | GLY | LYS | ASN | THR | ||||
| 3 | ALA | ASN | LEU | SER | LEU | ILE | THR | LYS | LEU | SER | ||||
| 4 | GLN | GLU | ASP | GLY | ALA | ILE | LEU | PHE | PRO | GLU | ||||
| 5 | ILE | ASP | ARG | TYR | SER | ASP | ASN | LYS | GLN | ILE | ||||
| 6 | LYS | ALA | LEU | THR | GLN | GLN | ILE | THR | LYS | VAL | ||||
| 7 | THR | VAL | ASN | GLY | THR | VAL | TYR | LYS | ASP | LEU | ||||
| 8 | ILE | SER | ASP | SER | VAL | LYS | ASP | THR | ASN | GLY | ||||
| 9 | TRP | VAL | SER | ASN | MET | THR | GLY | LEU | HIS | LEU | ||||
| 10 | GLY | THR | LYS | ALA | PHE | LYS | ASP | GLY | GLU | ASN | ||||
| 11 | THR | ILE | VAL | ILE | SER | SER | LYS | GLY | PHE | GLU | ||||
| 12 | ASP | VAL | THR | ILE | THR | VAL | THR | LYS | LYS | ASP | ||||
| 13 | GLY | GLN | ILE | HIS | PHE | VAL | SER | ALA | LYS | GLN | ||||
| 14 | LYS | GLN |
Samples:
sample_1: Shr-HID2, [U-100% 13C; U-100% 15N], 1.1 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.01%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 298 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHANH | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CARA, Keller and Wuthrich - chemical shift assignment
TOPSPIN, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker DRX 600 MHz
- Bruker DRX 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks