BMRB Entry 27550
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27550
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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 |
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