BMRB Entry 34865
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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/BMR34865
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NMR-STAR v3 text file.
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Title: Folded alpha helical de novo proteins from Apilactobacillus kunkeei PubMed: 38355092
Deposition date: 2023-09-27 Original release date: 2024-02-14
Authors: Celestine, C.
Citation: Ye, Weihua; Krishna Behra, Phani Rama; Dyrhage, Karl; Seeger, Christian; Joiner, Joe; Karlsson, Elin; Andersson, Eva; Chi, Celestine; Andersson, Siv; Jemth, Per. "Folded Alpha Helical Putative New Proteins from Apilactobacillus kunkeei" J. Mol. Biol. 436, 168490-168490 (2024).
Assembly members:
entity_1, polymer, 49 residues, 5860.950 Da.
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):
entity_1: GSMKNYQPNKDLLEILESQK
IKIKNLKEEVKILQRKIDQQ
IAKERVIKQ
- assigned_chemical_shifts
- spectral_peak_list
Data type | Count |
13C chemical shifts | 96 |
15N chemical shifts | 45 |
1H chemical shifts | 262 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 49 residues - 5860.950 Da.
1 | GLY | SER | MET | LYS | ASN | TYR | GLN | PRO | ASN | LYS | ||||
2 | ASP | LEU | LEU | GLU | ILE | LEU | GLU | SER | GLN | LYS | ||||
3 | ILE | LYS | ILE | LYS | ASN | LEU | LYS | GLU | GLU | VAL | ||||
4 | LYS | ILE | LEU | GLN | ARG | LYS | ILE | ASP | GLN | GLN | ||||
5 | ILE | ALA | LYS | GLU | ARG | VAL | ILE | LYS | GLN |
Samples:
sample_1: Orphan7, [U-99% 13C; U-99% 15N], 500 uM
sample_conditions_1: ionic strength: 150 mM; pH: 6.5; 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-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
CcpNmr Analysis, CCPN - peak picking
NMR spectrometers:
- Bruker AVANCE NEO 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts