BMRB Entry 50763
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50763
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Title: ARNT PAS-B Y456T sequence unfolded in 8M urea
Deposition date: 2021-02-12 Original release date: 2021-03-10
Authors: Xu, Xingjian; Dikiy, Igor; Evans, Matthew; Marcelino, Leandro; Gardner, Kevin
Citation: Xu, Xingjian; Dikiy, Igor; Evans, Matthew; Marcelino, Leandro; Gardner, Kevin. "Fragile protein folds: sequence and environmental factors affecting the equilibrium of two interconverting, stably folded protein conformations" Magn. Reson. 2, 63-76 (2021).
Assembly members:
entity_1, polymer, 119 residues, 13880.67 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHis-parallel
Entity Sequences (FASTA):
entity_1: GAMDNVCQPTEFISRHNIEG
IFTFVDHRCVATVGYQPQEL
LGKNIVEFCHPEDQQLLRDS
FQQVVKLKGQVLSVMFRFRS
KNQEWLWMRTSSFTFQNPYS
DEIETIICTNTNVKNSSQE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 349 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 112 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ARNT PAS-B Y456T urea unfolded | 1 |
Entities:
Entity 1, ARNT PAS-B Y456T urea unfolded 119 residues - 13880.67 Da.
N-terminal 4 residues (GAMD) are vector-derived; remaining sequence is residues 356-470 from human ARNT protein.
| 1 | GLY | ALA | MET | ASP | ASN | VAL | CYS | GLN | PRO | THR | ||||
| 2 | GLU | PHE | ILE | SER | ARG | HIS | ASN | ILE | GLU | GLY | ||||
| 3 | ILE | PHE | THR | PHE | VAL | ASP | HIS | ARG | CYS | VAL | ||||
| 4 | ALA | THR | VAL | GLY | TYR | GLN | PRO | GLN | GLU | LEU | ||||
| 5 | LEU | GLY | LYS | ASN | ILE | VAL | GLU | PHE | CYS | HIS | ||||
| 6 | PRO | GLU | ASP | GLN | GLN | LEU | LEU | ARG | ASP | SER | ||||
| 7 | PHE | GLN | GLN | VAL | VAL | LYS | LEU | LYS | GLY | GLN | ||||
| 8 | VAL | LEU | SER | VAL | MET | PHE | ARG | PHE | ARG | SER | ||||
| 9 | LYS | ASN | GLN | GLU | TRP | LEU | TRP | MET | ARG | THR | ||||
| 10 | SER | SER | PHE | THR | PHE | GLN | ASN | PRO | TYR | SER | ||||
| 11 | ASP | GLU | ILE | GLU | THR | ILE | ILE | CYS | THR | ASN | ||||
| 12 | THR | ASN | VAL | LYS | ASN | SER | SER | GLN | GLU |
Samples:
sample_1: ARNT PAS-B Y456T, [U-99% 13C; U-99% 15N], 500 uM; urea 8 M; TRIS 50 mM; sodium chloride 20 mM; beta-mercaptoethanol 5 mM
sample_conditions_1: pH: 7.5; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRViewJ - chemical shift assignment
NMRPipe - processing
VNMRj - collection
NMR spectrometers:
- Varian INOVA 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts