BMRB Entry 15795
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15795
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Citation: Salinas, Roberto; Camilo, Cesar; Tomaselli, Simona; Valencia, Estela; Farah, Chuck; El-Dorry, Hamza; Chambergo, Felipe. "Solution structure of the C-terminal domain of multiprotein bridging factor 1 (MBF1) of Trichoderma reesei" Proteins 75, 518-523 (2009).
PubMed: 19137618
Assembly members:
MBF1, polymer, 107 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pPROEX-HTa
Entity Sequences (FASTA):
MBF1: GAMDPEFAGGTEGQRLTKVD
RSDDIIKPKTVGKEVGKAIE
QGRQKFEPTMTQAELGKEIG
ETAATVASYERGTATPDQNI
LSKMERVLNVKLRGANIGAP
RLGPKKK
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- H_exch_protection_factors
| Data type | Count |
| 13C chemical shifts | 424 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 580 |
| heteronuclear NOE values | 82 |
| H exchange protection factors | 34 |
| T1 relaxation values | 71 |
| T2 relaxation values | 71 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MBF1 | 1 |
Entities:
Entity 1, MBF1 107 residues - Formula weight is not available
The protein construction has a fusion of 7 extra amino acids (GAMDPEF) due to the expression vector. Therefore, Ala8 corresponds to Ala56 in the full length protein.
| 1 | GLY | ALA | MET | ASP | PRO | GLU | PHE | ALA | GLY | GLY | ||||
| 2 | THR | GLU | GLY | GLN | ARG | LEU | THR | LYS | VAL | ASP | ||||
| 3 | ARG | SER | ASP | ASP | ILE | ILE | LYS | PRO | LYS | THR | ||||
| 4 | VAL | GLY | LYS | GLU | VAL | GLY | LYS | ALA | ILE | GLU | ||||
| 5 | GLN | GLY | ARG | GLN | LYS | PHE | GLU | PRO | THR | MET | ||||
| 6 | THR | GLN | ALA | GLU | LEU | GLY | LYS | GLU | ILE | GLY | ||||
| 7 | GLU | THR | ALA | ALA | THR | VAL | ALA | SER | TYR | GLU | ||||
| 8 | ARG | GLY | THR | ALA | THR | PRO | ASP | GLN | ASN | ILE | ||||
| 9 | LEU | SER | LYS | MET | GLU | ARG | VAL | LEU | ASN | VAL | ||||
| 10 | LYS | LEU | ARG | GLY | ALA | ASN | ILE | GLY | ALA | PRO | ||||
| 11 | ARG | LEU | GLY | PRO | LYS | LYS | LYS |
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