BMRB Entry 30284
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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/BMR30284
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Title: Backbone structure of the Yersinia pestis outer membrane protein Ail in phospholipid bilayer nanodisc PubMed: 28726410
Deposition date: 2017-04-19 Original release date: 2017-05-15
Authors: Dutta, S.; Yong, Y.; Marassi, F.
Citation: Dutta, S.; Yong, Y.; Marassi, F.. "Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers" J. Phys. Chem. B 121, 7561-7570 (2017).
Assembly members:
entity_1, polymer, 156 residues, 17492.400 Da.
Natural source: Common Name: Yersinia pestis Taxonomy ID: 632 Superkingdom: Bacteria Kingdom: not available Genus/species: Yersinia pestis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: EGESSISIGYAQSRVKEDGY
KLDKNPRGFNLKYRYEFNND
WGVIGSFAQTRRGFEESVDG
FKLIDGDFKYYSVTAGPVFR
INEYVSLYGLLGAGHGKAKF
SSIFGQSESRSKTSLAYGAG
LQFNPHPNFVIDASYEYSKL
DDVKVGTWMLGAGYRF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 94 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 91 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 156 residues - 17492.400 Da.
| 1 | GLU | GLY | GLU | SER | SER | ILE | SER | ILE | GLY | TYR | ||||
| 2 | ALA | GLN | SER | ARG | VAL | LYS | GLU | ASP | GLY | TYR | ||||
| 3 | LYS | LEU | ASP | LYS | ASN | PRO | ARG | GLY | PHE | ASN | ||||
| 4 | LEU | LYS | TYR | ARG | TYR | GLU | PHE | ASN | ASN | ASP | ||||
| 5 | TRP | GLY | VAL | ILE | GLY | SER | PHE | ALA | GLN | THR | ||||
| 6 | ARG | ARG | GLY | PHE | GLU | GLU | SER | VAL | ASP | GLY | ||||
| 7 | PHE | LYS | LEU | ILE | ASP | GLY | ASP | PHE | LYS | TYR | ||||
| 8 | TYR | SER | VAL | THR | ALA | GLY | PRO | VAL | PHE | ARG | ||||
| 9 | ILE | ASN | GLU | TYR | VAL | SER | LEU | TYR | GLY | LEU | ||||
| 10 | LEU | GLY | ALA | GLY | HIS | GLY | LYS | ALA | LYS | PHE | ||||
| 11 | SER | SER | ILE | PHE | GLY | GLN | SER | GLU | SER | ARG | ||||
| 12 | SER | LYS | THR | SER | LEU | ALA | TYR | GLY | ALA | GLY | ||||
| 13 | LEU | GLN | PHE | ASN | PRO | HIS | PRO | ASN | PHE | VAL | ||||
| 14 | ILE | ASP | ALA | SER | TYR | GLU | TYR | SER | LYS | LEU | ||||
| 15 | ASP | ASP | VAL | LYS | VAL | GLY | THR | TRP | MET | LEU | ||||
| 16 | GLY | ALA | GLY | TYR | ARG | PHE |
Samples:
sample_1: Ail, [U-13C; U-15N; U-2H], 0.66 mM; DMPC 49.5 mM; DMPG 16.5 mM; sodium chloride 5 mM; sodium phosphate 25 mM
sample_conditions_1: ionic strength: 10 mM; pH: 6.5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY-HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment
TOPSPIN, Bruker Biospin - processing
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMR spectrometers:
- Bruker AvanceIII 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts