BMRB Entry 15931
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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/BMR15931
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Title: Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form PubMed: 19679089
Deposition date: 2008-08-27 Original release date: 2009-09-03
Authors: Stott, Katherine
Citation: Stott, Katherine; Yusof, Adlina; Perham, Richard; Jones, Dafydd. "A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure" Structure 17, 1117-1127 (2009).
Assembly members:
E2plipD4, polymer, 85 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
Entity Sequences (FASTA):
E2plipD4: MVKEVNVPDIVEVTEVMVKV
GDKVAAEQSLITVEGDKASM
EVPAPFAGVVKELKVNVGDK
VKTGSLIMIFEVEGAAPAAA
PAKQE
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 72 |
| 1H chemical shifts | 495 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E2plipD4, chain 1 | 1 |
| 2 | E2plipD4, chain 2 | 1 |
Entities:
Entity 1, E2plipD4, chain 1 85 residues - Formula weight is not available
| 1 | MET | VAL | LYS | GLU | VAL | ASN | VAL | PRO | ASP | ILE | ||||
| 2 | VAL | GLU | VAL | THR | GLU | VAL | MET | VAL | LYS | VAL | ||||
| 3 | GLY | ASP | LYS | VAL | ALA | ALA | GLU | GLN | SER | LEU | ||||
| 4 | ILE | THR | VAL | GLU | GLY | ASP | LYS | ALA | SER | MET | ||||
| 5 | GLU | VAL | PRO | ALA | PRO | PHE | ALA | GLY | VAL | VAL | ||||
| 6 | LYS | GLU | LEU | LYS | VAL | ASN | VAL | GLY | ASP | LYS | ||||
| 7 | VAL | LYS | THR | GLY | SER | LEU | ILE | MET | ILE | PHE | ||||
| 8 | GLU | VAL | GLU | GLY | ALA | ALA | PRO | ALA | ALA | ALA | ||||
| 9 | PRO | ALA | LYS | GLN | GLU |
Samples:
sample_1: E2plipD4, [U-15N], 1 mM; sodium phosphate 20 mM; TSP 40 uM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O, . - structure solution
NMR spectrometers:
- Bruker DRX 500 MHz
Related Database Links:
| PDB | |
| EMBL | CSG13687 CSG39424 |
| GB | EFI22553 EGB41640 EGI23519 EGI24249 EGI43488 |
| REF | WP_000374927 WP_032230881 WP_050541395 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts