BMRB Entry 27837
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27837
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for RepA PubMed: 31918960
Deposition date: 2019-03-15 Original release date: 2019-12-17
Authors: Pantoja-Uceda, David; Oroz, Javier; Laurents, Douglas
Citation: Pantoja-Uceda, David; Oroz, Javier; Fernandez, Cristina; de Alba, Eva; Giraldo, Rafael; Laurents, Douglas. "Conformational Priming of RepA-WH1 for Functional Amyloid Conversion Detected by NMR Spectroscopy" Structure 28, 336-347 (2020).
Assembly members:
RepA, polymer, 132 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pRG-H6-WH1
Entity Sequences (FASTA):
RepA: MVENQVTQSNKLIESSHTLT
LNEKRLVLCAASLIDSRKPL
PKDGYLTIRADTFAEVFGID
VKHAYAALDDAATKLFNRDI
RRYVKGKVVERMRWVFHVKY
REGQGCVELGFSPTIIPHLT
MLHKEFTSYQLK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 390 |
| 15N chemical shifts | 126 |
| 1H chemical shifts | 126 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RepA chain 1 | 1 |
| 2 | RepA chain 2 | 1 |
Entities:
Entity 1, RepA chain 1 132 residues - Formula weight is not available
| 1 | MET | VAL | GLU | ASN | GLN | VAL | THR | GLN | SER | ASN | ||||
| 2 | LYS | LEU | ILE | GLU | SER | SER | HIS | THR | LEU | THR | ||||
| 3 | LEU | ASN | GLU | LYS | ARG | LEU | VAL | LEU | CYS | ALA | ||||
| 4 | ALA | SER | LEU | ILE | ASP | SER | ARG | LYS | PRO | LEU | ||||
| 5 | PRO | LYS | ASP | GLY | TYR | LEU | THR | ILE | ARG | ALA | ||||
| 6 | ASP | THR | PHE | ALA | GLU | VAL | PHE | GLY | ILE | ASP | ||||
| 7 | VAL | LYS | HIS | ALA | TYR | ALA | ALA | LEU | ASP | ASP | ||||
| 8 | ALA | ALA | THR | LYS | LEU | PHE | ASN | ARG | ASP | ILE | ||||
| 9 | ARG | ARG | TYR | VAL | LYS | GLY | LYS | VAL | VAL | GLU | ||||
| 10 | ARG | MET | ARG | TRP | VAL | PHE | HIS | VAL | LYS | TYR | ||||
| 11 | ARG | GLU | GLY | GLN | GLY | CYS | VAL | GLU | LEU | GLY | ||||
| 12 | PHE | SER | PRO | THR | ILE | ILE | PRO | HIS | LEU | THR | ||||
| 13 | MET | LEU | HIS | LYS | GLU | PHE | THR | SER | TYR | GLN | ||||
| 14 | LEU | LYS |
Samples:
sample_1: RepA, [U-99% 13C; U-99% 15N], 1.0 mM; deuterated acetic acid 1.0 mM; mQ 85%; D2O 15%; DSS 50 uM
sample_conditions_1: ionic strength: 0.001 M; pH: 4.0; pressure: 1 atm; temperature: 323.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO trosy | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO trosy | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA trosy | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA trosy | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCACONH trosy | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB trosy | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection
NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView v5.0, Johnson, One Moon Scientific - data analysis, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts