BMRB Entry 16090
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16090
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Title: NMR Structure of a Monomeric Folding Intermediate Reveals the Structural Basis for Rapid Assembly of an Evolutionary Optimized Trimerization Module PubMed: 19361528
Deposition date: 2008-12-24 Original release date: 2009-04-22
Authors: Habazettl, Judith; Reiner, Andreas; Kiefhaber, Thomas
Citation: Habazettl, Judith; Reiner, Andreas; Kiefhaber, Thomas. "NMR Structure of a Monomeric Intermediate on the Evolutionarily Optimized Assembly Pathway of a Small Trimerization Domain" J. Mol. Biol. 389, 103-114 (2009).
Assembly members:
foldon_E5R, polymer, 29 residues, 3112.573 Da.
Natural source: Common Name: Enterobacteria phage T4 sensu lato Taxonomy ID: 348604 Superkingdom: Viruses Kingdom: not available Genus/species: T4-like viruses Enterobacteria phage T4 sensu lato
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
foldon_E5R: GSGYIPRAPRDGQAYVRKDG
EWVLLSTFL
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 26 |
| 1H chemical shifts | 192 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | foldon_E5R | 1 |
Entities:
Entity 1, foldon_E5R 29 residues - 3112.573 Da.
residues 1-27 represent the residues 458-484 in native fibritin
| 1 | GLY | SER | GLY | TYR | ILE | PRO | ARG | ALA | PRO | ARG | ||||
| 2 | ASP | GLY | GLN | ALA | TYR | VAL | ARG | LYS | ASP | GLY | ||||
| 3 | GLU | TRP | VAL | LEU | LEU | SER | THR | PHE | LEU |
Samples:
sample_1: foldon E5R 200 uM; K_3 PO_4 10 mM
sample_2: foldon E5R, [U-99% 15N], 210 uM; K_3 PO_4 10 mM
sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1 atm; temperature: 296.7 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker - data analysis
SPARKY, Goddard - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
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