BMRB Entry 15478
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15478
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Title: 1H and 15N resonance assignment of M7, a computationally-designed artificial protein PubMed: 18498106
Deposition date: 2007-09-19 Original release date: 2008-06-25
Authors: Stordeur, Claudius; Dalluege, Roman; Birkenmeier, Olaf; Wienk, Hans; Rudolph, Rainer; Lange, Christian; Luecke, Christian
Citation: Stordeur, Claudius; Dalluege, Roman; Birkenmeier, Olaf; Wienk, Hans; Rudolph, Rainer; Lange, Christian; Luecke, Christian. "The NMR solution structure of the artificial protein M7 matches the computationally designed model" Proteins 72, 1104-1107 (2008).
Assembly members:
M7, polymer, 96 residues, 10820.4 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not applicable
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
M7: GSHMKVDITIKIQRDGQEIE
IDIRVSTGKELERALQELEK
ALARAGARNVQITISAENDE
QAKELLELIARLLQKLGYKD
INVRVNGTEVKIEVRV
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 728 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | M7 | 1 |
Entities:
Entity 1, M7 96 residues - 10820.4 Da.
The first four residues GSHM represent a cloning artifact; the protein sequence starts at Lys1.
| 1 | GLY | SER | HIS | MET | LYS | VAL | ASP | ILE | THR | ILE | ||||
| 2 | LYS | ILE | GLN | ARG | ASP | GLY | GLN | GLU | ILE | GLU | ||||
| 3 | ILE | ASP | ILE | ARG | VAL | SER | THR | GLY | LYS | GLU | ||||
| 4 | LEU | GLU | ARG | ALA | LEU | GLN | GLU | LEU | GLU | LYS | ||||
| 5 | ALA | LEU | ALA | ARG | ALA | GLY | ALA | ARG | ASN | VAL | ||||
| 6 | GLN | ILE | THR | ILE | SER | ALA | GLU | ASN | ASP | GLU | ||||
| 7 | GLN | ALA | LYS | GLU | LEU | LEU | GLU | LEU | ILE | ALA | ||||
| 8 | ARG | LEU | LEU | GLN | LYS | LEU | GLY | TYR | LYS | ASP | ||||
| 9 | ILE | ASN | VAL | ARG | VAL | ASN | GLY | THR | GLU | VAL | ||||
| 10 | LYS | ILE | GLU | VAL | ARG | VAL |
Samples:
sample_1: M7 1.0 mM; sodium phosphate 25 mM; sodium azide 0.05%; H2O 95%; D2O 5%
sample_2: M7, [U-98% 15N], 1.3 mM; sodium phosphate 25 mM; sodium azide 0.05%; H2O 95%; D2O 5%
sample_3: M7 1.0 mM; sodium phosphate 25 mM; sodium azide 0.05%; D2O 100%
sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HTQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
xwinnmr v3.5, Bruker Biospin - collection, processing
FELIX v2000, Accelrys Software Inc. - data analysis
DYANA v1.5, Guntert, Braun and Wuthrich - structure solution
DISCOVER v2000, Accelrys Software Inc. - refinement
NMR spectrometers:
- Bruker DRX 500 MHz
Related Database Links:
| PDB |
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