BMRB Entry 25909
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25909
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Title: 1H, 13C, and 15N Chemical Shift Assignments for in vitro GB1 PubMed: 27910948
Deposition date: 2015-11-26 Original release date: 2016-12-21
Authors: Ikeya, Teppei; Hanashima, Tomomi; Hosoya, Saori; Shimazaki, Manato; Ikeda, Shiro; Mishima, Masaki; Guentert, Peter; Ito, Yutaka
Citation: Ikeya, Teppei; Hanashima, Tomomi; Hosoya, Saori; Shimazaki, Manato; Ikeda, Shiro; Mishima, Masaki; Guentert, Peter; Ito, Yutaka. "Improved in-cell structure determination of proteins at near-physiological concentration" Sci. Rep. 6, 38312-38312 (2016).
Assembly members:
entity, polymer, 57 residues, 6258.896 Da.
Natural source: Common Name: firmicutes Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MGTYKLILNGKTLKGETTTE
AVDAATAEKVFKQYANDNGV
DGEWTYDDATKTFTVTE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 251 |
| 15N chemical shifts | 62 |
| 1H chemical shifts | 384 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 57 residues - 6258.896 Da.
| 1 | MET | GLY | THR | TYR | LYS | LEU | ILE | LEU | ASN | GLY | ||||
| 2 | LYS | THR | LEU | LYS | GLY | GLU | THR | THR | THR | GLU | ||||
| 3 | ALA | VAL | ASP | ALA | ALA | THR | ALA | GLU | LYS | VAL | ||||
| 4 | PHE | LYS | GLN | TYR | ALA | ASN | ASP | ASN | GLY | VAL | ||||
| 5 | ASP | GLY | GLU | TRP | THR | TYR | ASP | ASP | ALA | THR | ||||
| 6 | LYS | THR | PHE | THR | VAL | THR | GLU |
Samples:
sample_1: Protein G B1, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.31 M; pH: 7.0; pressure: 1 atm; temperature: 295 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 CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure solution
AZARA v2.8.1, Boucher - processing
TALOS v1, Cornilescu, Delaglio and Bax - chemical shift calculation
OPAL v1.4, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
Molmol v2.6, Koradi, Billeter and Wuthrich - structure solution
ANSIG v3.3, Kraulis - chemical shift assignment
TOPSPIN v3.1, Bruker Biospin - collection
CcpNMR, CCPN - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts