BMRB Entry 30623
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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/BMR30623
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: Solution structure of the C-terminal zinc finger of the C. elegans protein MEX-5 PubMed: 32294479
Deposition date: 2019-07-01 Original release date: 2020-04-27
Authors: Massi, F.; Tavella, D.
Citation: Tavella, Davide; Ertekin, Asli; Schaal, Hila; Ryder, Sean; Massi, Francesca. "A Disorder-to-Order Transition Mediates RNA Binding of the Caenorhabditis elegans Protein MEX-5" Biophys. J. 118, 2001-2014 (2020).
Assembly members:
entity_1, polymer, 35 residues, 4031.641 Da.
entity_ZN, non-polymer, 65.409 Da.
Natural source: Common Name: C. elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: NNKYKTKLCKNFARGGTGFC
PYGLRCEFVHPTDKE
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 114 |
| 15N chemical shifts | 32 |
| 1H chemical shifts | 222 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 35 residues - 4031.641 Da.
| 1 | ASN | ASN | LYS | TYR | LYS | THR | LYS | LEU | CYS | LYS | ||||
| 2 | ASN | PHE | ALA | ARG | GLY | GLY | THR | GLY | PHE | CYS | ||||
| 3 | PRO | TYR | GLY | LEU | ARG | CYS | GLU | PHE | VAL | HIS | ||||
| 4 | PRO | THR | ASP | LYS | GLU |
Entity 2, entity_2 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: MEX-5, [U-13C; U-15N], 300 nM
sample_conditions_1: ionic strength: 100 mM; pH: 6.2; pressure: 1 atm; temperature: 294 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 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
Sparky, Goddard - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts