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 |
Samples:
sample_1: MBF1, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 50 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.05 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 | 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView v5.2.2, CCPN, Johnson, One Moon Scientific - chemical shift assignment, chemical shift assignment, peak picking
NMR spectrometers:
- Varian INOVA 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