BMRB Entry 30422
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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/BMR30422
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Title: Solution structure of the zebrafish granulin AaE PubMed: 29732682
Deposition date: 2018-02-28 Original release date: 2018-06-07
Authors: Wang, P.; Ni, F.
Citation: Wang, P.; Chitramuthu, B.; Bateman, A.; Bennett, H.; Xu, P.; Ni, F.. "Structure Dissection of Zebrafish Progranulins Identifies a Well-Folded Granulin/Epithelin Module Protein with pro-Cell Survival Activities" Protein Science 27, 1476-1490 (2018).
Assembly members:
entity_1, polymer, 56 residues, 5698.431 Da.
Natural source: Common Name: Zebrafish Taxonomy ID: 7955 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Danio rerio
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: DVQCGGGFSCHDGETCCPTS
QTTWGCCPSPKAVCCDDMQH
CCPAGYKCGPGGTCIS
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 55 |
1H chemical shifts | 302 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 56 residues - 5698.431 Da.
1 | ASP | VAL | GLN | CYS | GLY | GLY | GLY | PHE | SER | CYS | ||||
2 | HIS | ASP | GLY | GLU | THR | CYS | CYS | PRO | THR | SER | ||||
3 | GLN | THR | THR | TRP | GLY | CYS | CYS | PRO | SER | PRO | ||||
4 | LYS | ALA | VAL | CYS | CYS | ASP | ASP | MET | GLN | HIS | ||||
5 | CYS | CYS | PRO | ALA | GLY | TYR | LYS | CYS | GLY | PRO | ||||
6 | GLY | GLY | THR | CYS | ILE | SER |
Samples:
sample_1: zebrafish granulin AaE 0.5 mM; sodium chloride 150 mM; EDTA 0.2 mM
sample_2: zebrafish granulin AaE, [U-15N], 0.5 mM; sodium chloride 150 mM; EDTA 0.2 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 760 mmHg; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | anisotropic | sample_conditions_1 |
Software:
CNS v1.0, Brunger et al. - refinement, structure calculation
ARIA, Nilges et al. - refinement, structure calculation
NMRView, Johnson et al. - chemical shift assignment
NMRview, Johnson et al. - peak picking
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts