BMRB Entry 5222
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5222
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Citation: Krumme, Dirk; Hecht, Hans-Jurgen; Menge, Ulrich; Ross, Anton; Wray, Victor; Flohe, Leopold. "Letter to the Editor: 1H, 15N and 13C resonance assignments and secondary
structure of Tryparedoxin-I from Crithidia fasciculata" J. Biomol. NMR 22, 375-376 (2002).
PubMed: 12018487
Assembly members:
tryparedoxin I, polymer, 153 residues, Formula weight is not available
Natural source: Common Name: Crithidia fasciculata Taxonomy ID: 5656 Superkingdom: Eukaryota Kingdom: not available Genus/species: Crithidia fasciculata
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b(+)
Entity Sequences (FASTA):
tryparedoxin I: SGLDKYLPGIEKLRRGDGEV
EVKSLAGKLVFFYFSASWCP
PCRGFTPQLIEFYDKFHESK
NFEVVFCTWDEEEDGFAGYF
AKMPWLAVPFAQSEAVQKLS
KHFNVESIPTLIGVDADSGD
VVTTRARATLVKDPEGEQFP
WKDAPLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 404 |
| 15N chemical shifts | 133 |
| 1H chemical shifts | 824 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | tryparedoxin I | 1 |
Entities:
Entity 1, tryparedoxin I 153 residues - Formula weight is not available
| 1 | SER | GLY | LEU | ASP | LYS | TYR | LEU | PRO | GLY | ILE | ||||
| 2 | GLU | LYS | LEU | ARG | ARG | GLY | ASP | GLY | GLU | VAL | ||||
| 3 | GLU | VAL | LYS | SER | LEU | ALA | GLY | LYS | LEU | VAL | ||||
| 4 | PHE | PHE | TYR | PHE | SER | ALA | SER | TRP | CYS | PRO | ||||
| 5 | PRO | CYS | ARG | GLY | PHE | THR | PRO | GLN | LEU | ILE | ||||
| 6 | GLU | PHE | TYR | ASP | LYS | PHE | HIS | GLU | SER | LYS | ||||
| 7 | ASN | PHE | GLU | VAL | VAL | PHE | CYS | THR | TRP | ASP | ||||
| 8 | GLU | GLU | GLU | ASP | GLY | PHE | ALA | GLY | TYR | PHE | ||||
| 9 | ALA | LYS | MET | PRO | TRP | LEU | ALA | VAL | PRO | PHE | ||||
| 10 | ALA | GLN | SER | GLU | ALA | VAL | GLN | LYS | LEU | SER | ||||
| 11 | LYS | HIS | PHE | ASN | VAL | GLU | SER | ILE | PRO | THR | ||||
| 12 | LEU | ILE | GLY | VAL | ASP | ALA | ASP | SER | GLY | ASP | ||||
| 13 | VAL | VAL | THR | THR | ARG | ALA | ARG | ALA | THR | LEU | ||||
| 14 | VAL | LYS | ASP | PRO | GLU | GLY | GLU | GLN | PHE | PRO | ||||
| 15 | TRP | LYS | ASP | ALA | PRO | LEU | GLU | HIS | HIS | HIS | ||||
| 16 | HIS | HIS | HIS |
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