BMRB Entry 15565
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15565
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Citation: Codutti, Luca; Picotti, Paola; Marin, Oriano; Dewilde, Sylvia; Fogolari, Federico; Corazza, Alessandra; Viglino, Paolo; Moens, Luc; Esposito, Gennaro; Fontana, Angelo. "Conformational stability of neuroglobin helix F--possible effects on the folding pathway within the globin family" FEBS J. 276, 5177-5190 (2009).
PubMed: 19674102
Assembly members:
Neuroglobin_HelixF, polymer, 24 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis Host organism: no host
Entity Sequences (FASTA):
Neuroglobin_HelixF: XVEDLSSLEEYLASLGRKHR
AVGX
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 404 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Neuroglobin HelixF | 1 |
Entities:
Entity 1, Neuroglobin HelixF 24 residues - Formula weight is not available
Residues are numbered according Human Neuroglobin Sequence. N-terminal and C-terminal residues are capped
| 1 | ACE | VAL | GLU | ASP | LEU | SER | SER | LEU | GLU | GLU | ||||
| 2 | TYR | LEU | ALA | SER | LEU | GLY | ARG | LYS | HIS | ARG | ||||
| 3 | ALA | VAL | GLY | NH2 |
Samples:
sample_1: Neuroglobin HelixF 1.2 ± 0.1 mM; sodium azide 0.1 ± 0.05 %; sodium chloride 100 ± 1 mM; dioxane 13 ± 1 mM; D2O 10 ± 0.1 %; sodium phosphate 70 ± 1 mM
sample_2: Neuroglobin HelixF 1.2 ± 0.1 mM; sodium azide 0.1 ± 0.05 %; sodium chloride 100 ± 1 mM; dioxane 13 ± 1 mM; D2O 10 ± 0.1 %; sodium phosphate 70 ± 1 mM
sample_3: Neuroglobin HelixF 1.2 ± 0.1 mM; sodium azide 0.1 ± 0.05 %; sodium chloride 100 ± 1 mM; dioxane 13 ± 1 mM; D2O 10 ± 0.1 %; sodium phosphate 70 ± 1 mM; TFE, [U-2H], 10 ± 1 %
sample_conditions_1: temperature: 298 K; pH: 6.3; pressure: 1 atm; ionic strength: 170 mM
sample_conditions_2: pH: 2.1; temperature: 298 K; ionic strength: 170 mM
sample_conditions_3: temperature: 298 K; pH: 6.3; pressure: 1 atm; ionic strength: 170 mM; dielectric constant: 72.9 none
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 2D DQF-COSY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_3 |
| 2D DQF-COSY | sample_3 | isotropic | sample_conditions_3 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_3 |
| 2D 1H-1H ROESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H ROESY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H ROESY | sample_3 | isotropic | sample_conditions_3 |
Software:
Felix v2000, Accelrys Software Inc. - chemical shift assignment, peak picking, processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization
DISCOVER, Accelrys Software Inc. - refinement
ProcheckNMR, Laskowski and MacArthur - structure evaluation
TOPSPIN v1.3, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 500 MHz