BMRB Entry 25346
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25346
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Title: MG200 EAGR box PubMed: 25471372
Deposition date: 2014-11-14 Original release date: 2014-12-16
Authors: Lalli, Daniela; Martinelli, Luca; Garcia-Morales, Luis; Ratera, Merce; Querol, Enrique; Pinol, Jaume; Fita, Ignacio; Calisto, Barbara
Citation: Martinelli, Luca; Lalli, Daniela; Garcia-Morales, Luis; Ratera, Merce; Querol, Enrique; Pinol, Jaume; Fita, Ignacio; Calisto, Barbara. "A major determinant for gliding motility in Mycoplasma genitalium: the interaction between the terminal organelle proteins MG200 and MG491" J. Biol. Chem. 290, 1699-1711 (2015).
Assembly members:
MG200_EAGR_box, polymer, 94 residues, Formula weight is not available
Natural source: Common Name: mycoplasmas Taxonomy ID: 2097 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycoplasma Genitalium
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MG200_EAGR_box: MAKQEQPEINLDHVVEQTIK
KVQQNQNQNKDPDELRSKVP
GEVTASDWEALVGDTRYGYF
DETGDWSWKGYFDEQGKWVW
NEPVDSLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 317 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 224 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MG200 EAGRbox | 1 |
Entities:
Entity 1, MG200 EAGRbox 94 residues - Formula weight is not available
Construct residues 122-123 and 210-215 were added for cloning purposes and are not part of the domain native sequence
| 1 | MET | ALA | LYS | GLN | GLU | GLN | PRO | GLU | ILE | ASN | ||||
| 2 | LEU | ASP | HIS | VAL | VAL | GLU | GLN | THR | ILE | LYS | ||||
| 3 | LYS | VAL | GLN | GLN | ASN | GLN | ASN | GLN | ASN | LYS | ||||
| 4 | ASP | PRO | ASP | GLU | LEU | ARG | SER | LYS | VAL | PRO | ||||
| 5 | GLY | GLU | VAL | THR | ALA | SER | ASP | TRP | GLU | ALA | ||||
| 6 | LEU | VAL | GLY | ASP | THR | ARG | TYR | GLY | TYR | PHE | ||||
| 7 | ASP | GLU | THR | GLY | ASP | TRP | SER | TRP | LYS | GLY | ||||
| 8 | TYR | PHE | ASP | GLU | GLN | GLY | LYS | TRP | VAL | TRP | ||||
| 9 | ASN | GLU | PRO | VAL | ASP | SER | LEU | GLU | HIS | HIS | ||||
| 10 | HIS | HIS | HIS | HIS |
Samples:
sample_1: MG200 EAGR box, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.12 M; pH: 6.5; 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 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | 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:
TOPSPIN v2.0, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts