BMRB Entry 19053
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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/BMR19053
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Title: Solution structure of FimA wt PubMed: 24184277
Deposition date: 2013-02-24 Original release date: 2013-11-11
Authors: Walczak, Michal; Puorger, Chasper; Glockshuber, Rudi; Wider, Gerhard
Citation: Walczak, Michal; Puorger, Chasper; Glockshuber, Rudi; Wider, Gerhard. "Intramolecular Donor Strand Complementation in the E. coli Type 1 Pilus Subunit FimA Explains the Existence of FimA Monomers As Off-Pathway Products of Pilus Assembly That Inhibit Host Cell Apoptosis." J. Mol. Biol. 426, 542-549 (2014).
Assembly members:
FimA_wt, polymer, 159 residues, 15835.380 Da.
Natural source: Common Name: Enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
FimA_wt: AATTVNGGTVHFKGEVVNAA
CAVDAGSVDQTVQLGQVRTA
SLAQEGATSSAVGFNIQLND
CDTNVASKAAVAFLGTAIDA
GHTNVLALQSSAAGSATNVG
VQILDRTGAALTLDGATFSS
ETTLNNGTNTIPFQARYFAT
GAATPGAANADATFKVQYQ
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 668 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FimA wt | 1 |
Entities:
Entity 1, FimA wt 159 residues - 15835.380 Da.
| 1 | ALA | ALA | THR | THR | VAL | ASN | GLY | GLY | THR | VAL | ||||
| 2 | HIS | PHE | LYS | GLY | GLU | VAL | VAL | ASN | ALA | ALA | ||||
| 3 | CYS | ALA | VAL | ASP | ALA | GLY | SER | VAL | ASP | GLN | ||||
| 4 | THR | VAL | GLN | LEU | GLY | GLN | VAL | ARG | THR | ALA | ||||
| 5 | SER | LEU | ALA | GLN | GLU | GLY | ALA | THR | SER | SER | ||||
| 6 | ALA | VAL | GLY | PHE | ASN | ILE | GLN | LEU | ASN | ASP | ||||
| 7 | CYS | ASP | THR | ASN | VAL | ALA | SER | LYS | ALA | ALA | ||||
| 8 | VAL | ALA | PHE | LEU | GLY | THR | ALA | ILE | ASP | ALA | ||||
| 9 | GLY | HIS | THR | ASN | VAL | LEU | ALA | LEU | GLN | SER | ||||
| 10 | SER | ALA | ALA | GLY | SER | ALA | THR | ASN | VAL | GLY | ||||
| 11 | VAL | GLN | ILE | LEU | ASP | ARG | THR | GLY | ALA | ALA | ||||
| 12 | LEU | THR | LEU | ASP | GLY | ALA | THR | PHE | SER | SER | ||||
| 13 | GLU | THR | THR | LEU | ASN | ASN | GLY | THR | ASN | THR | ||||
| 14 | ILE | PRO | PHE | GLN | ALA | ARG | TYR | PHE | ALA | THR | ||||
| 15 | GLY | ALA | ALA | THR | PRO | GLY | ALA | ALA | ASN | ALA | ||||
| 16 | ASP | ALA | THR | PHE | LYS | VAL | GLN | TYR | GLN |
Samples:
sample_1: FimA_wt, [U-99% 13C; U-99% 15N], 2 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 0.08 M; pH: 7; pressure: 1 atm; temperature: 273 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 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N 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:
SPARKY, Brunger, Adams, Clore, Gros, Nilges and Read, Goddard, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, refinement, structure solution
NMR spectrometers:
- Bruker Avance 750 MHz
- Bruker Avance 900 MHz