BMRB Entry 34240
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34240
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Title: Protein environment affects the water-tryptophan binding mode. Molecular dynamics simulations of Engrailed homeodomain mutants PubMed: 29696277
Deposition date: 2018-03-02 Original release date: 2019-03-28
Authors: Trosanova, Z.; Zachrdla, M.; Jansen, S.; Srb, P.; Zidek, L.; Kozelka, J.
Citation: Spackova, N.; Trosanova, Z.; Sebesta, F.; Jansen, S.; Burda, J.; Srb, P.; Zachrdla, M.; Zidek, L.; Kozelka, J.. "Protein environment affects the water-tryptophan binding mode. MD, QM/MM, and NMR studies of engrailed homeodomain mutants." Phys. Chem. Chem. Phys. 20, 12664-12677 (2018).
Assembly members:
entity_1, polymer, 64 residues, 7626.657 Da.
entity_HOH, water, 18.015 Da.
Natural source: Common Name: Fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GAMEKRPRTAFSSEQLARLK
REFNENRYLTERRRQQLSSE
LGLNEAQIKIWFQNERAKIK
KSGS
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 466 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 64 residues - 7626.657 Da.
| 1 | GLY | ALA | MET | GLU | LYS | ARG | PRO | ARG | THR | ALA | ||||
| 2 | PHE | SER | SER | GLU | GLN | LEU | ALA | ARG | LEU | LYS | ||||
| 3 | ARG | GLU | PHE | ASN | GLU | ASN | ARG | TYR | LEU | THR | ||||
| 4 | GLU | ARG | ARG | ARG | GLN | GLN | LEU | SER | SER | GLU | ||||
| 5 | LEU | GLY | LEU | ASN | GLU | ALA | GLN | ILE | LYS | ILE | ||||
| 6 | TRP | PHE | GLN | ASN | GLU | ARG | ALA | LYS | ILE | LYS | ||||
| 7 | LYS | SER | GLY | SER |
Entity 2, entity_2 - 18.015 Da.
| 1 | HOH |
Samples:
sample_1: EnHD_K52E 1 mM
sample_conditions_1: ionic strength: 150 mM; pH: 5.7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | anisotropic | 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, peak picking
NMR spectrometers:
- Bruker AvanceIII 850 MHz