BMRB Entry 30204
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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/BMR30204
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Title: Solution structure of the de novo mini protein gHH_44
Deposition date: 2016-11-15 Original release date: 2017-09-25
Authors: Buchko, G.; Bahl, C.; Baker, D.
Citation: Bahl, C.; Buchko, G.; Baker, D.. "Biophysical characterization of hyperstable constrained peptides." . ., .-..
Assembly members:
entity_1, polymer, 28 residues, 3366.862 Da.
Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: AEDCERIRKELEKNPNDEIK
KKLEKCQA
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 117 |
| 15N chemical shifts | 29 |
| 1H chemical shifts | 164 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 28 residues - 3366.862 Da.
| 1 | ALA | GLU | ASP | CYS | GLU | ARG | ILE | ARG | LYS | GLU | ||||
| 2 | LEU | GLU | LYS | ASN | PRO | ASN | ASP | GLU | ILE | LYS | ||||
| 3 | LYS | LYS | LEU | GLU | LYS | CYS | GLN | ALA |
Samples:
sample_1: HH2, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium acetate, none, 25 ± 1 mM; sodium chloride, none, 50 ± 2 mM
sample_2: HH2, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium acetate, none, 25 ± 1 mM; sodium chloride, none, 50 ± 2 mM
sample_conditions_1: ionic strength: 0.075 M; pH: 4.8; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D C(CO)NH | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | anisotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | anisotropic | sample_conditions_1 |
| D20 exchange | sample_2 | anisotropic | sample_conditions_1 |
Software:
CNS v1.1, Brunger A. T. et.al. - refinement
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
Felix v2007, Accelrys Software Inc. - processing
PSVS v1.5, Bhattacharya and Montelione - chemical shift assignment
SPARKY v3.115, Goddard - data analysis
NMR spectrometers:
- Varian VXRS 600 MHz
- Varian VXRS 800 MHz
- Varian INOVA 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts