BMRB Entry 18565
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18565
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Title: Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin PubMed: 23765284
Deposition date: 2012-07-01 Original release date: 2014-02-11
Authors: Brothers, Michael; Geissler, Brett; Hisao, Grant; Satchell, Karla; Wilson, Brenda; Rienstra, Chad
Citation: Brothers, Michael; Geissler, Brett; Hisao, Grant; Satchell, Karla; Wilson, Brenda; Rienstra, Chad. "Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin." Biomol. NMR Assignments 8, 221-224 (2014).
Assembly members:
MLD_PMT, polymer, 90 residues, 10.5 Da.
Natural source: Common Name: g-proteobacteria Taxonomy ID: 747 Superkingdom: Bacteria Kingdom: not available Genus/species: Pasteurella multocida
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MLD_PMT: MGVWTPEVLKARASVIGKPI
GESYKRILAKLQRIHNSNIL
DERQGLMHELMELIDLYEES
QPSSERLNAFRELRTQLEKA
LGLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 366 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 568 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MLD PMT | 1 |
Entities:
Entity 1, MLD PMT 90 residues - 10.5 Da.
| 1 | MET | GLY | VAL | TRP | THR | PRO | GLU | VAL | LEU | LYS | |
| 2 | ALA | ARG | ALA | SER | VAL | ILE | GLY | LYS | PRO | ILE | |
| 3 | GLY | GLU | SER | TYR | LYS | ARG | ILE | LEU | ALA | LYS | |
| 4 | LEU | GLN | ARG | ILE | HIS | ASN | SER | ASN | ILE | LEU | |
| 5 | ASP | GLU | ARG | GLN | GLY | LEU | MET | HIS | GLU | LEU | |
| 6 | MET | GLU | LEU | ILE | ASP | LEU | TYR | GLU | GLU | SER | |
| 7 | GLN | PRO | SER | SER | GLU | ARG | LEU | ASN | ALA | PHE | |
| 8 | ARG | GLU | LEU | ARG | THR | GLN | LEU | GLU | LYS | ALA | |
| 9 | LEU | GLY | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: MLD PMT, [U-99% 13C; U-99% 15N], 1 mM; Bis-Tris 20 mM; sodium chloride 100 mM; EDTA 1 mM; sodium azide 0.01 mM; DSS 0.01 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment, data analysis
VNMRJ, Varian - collection
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| EMBL | CAA35885 CAA36717 CAA40921 CAA82233 CAD92744 |
| GB | AAL55665 AAW57319 AAX76908 ABR23002 ACG56672 |
| PRF | 1703272A |
| REF | WP_015691094 |
| SP | P17452 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts