BMRB Entry 34385
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34385
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Title: Solution Structure of ribosome-binding factor A (RbfA) under physiological conditions
Deposition date: 2019-04-01 Original release date: 2020-05-29
Authors: Schedlbauer, A.; Ochoa Lizarralde, B.; Capuni, R.; Iturrioz, I.; Fucini, P.; Connell, S.
Citation: Schedlbauer, A.; Ochoa Lizarralde, B.; Capuni, R.; Iturrioz, I.; Fucini, P.; Connell, S.. "Structural of Ribosomal States associated with late stage assembly factors" . ., .-..
Assembly members:
entity_1, polymer, 140 residues, 15933.329 Da.
Natural source: Common Name: Enterobacter sp. EC-NT1 Taxonomy ID: 2163603 Superkingdom: Bacteria Kingdom: not available Genus/species: Enterobacter Enterobacter sp. EC-NT1
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: SAKEFGRPQRVAQEMQKEIA
LILQREIKDPRLGMMTTVSG
VEMSRDLAYAKVYVTFLNDK
DEDAVKAGIKALQEASGFIR
SLLGKAMRLRIVPELTFFYD
NSLVEGMRMSNLVTSVVKHD
EERRVNPDDSKEDALEVLFQ
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 522 |
15N chemical shifts | 114 |
1H chemical shifts | 836 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 140 residues - 15933.329 Da.
1 | SER | ALA | LYS | GLU | PHE | GLY | ARG | PRO | GLN | ARG | |
2 | VAL | ALA | GLN | GLU | MET | GLN | LYS | GLU | ILE | ALA | |
3 | LEU | ILE | LEU | GLN | ARG | GLU | ILE | LYS | ASP | PRO | |
4 | ARG | LEU | GLY | MET | MET | THR | THR | VAL | SER | GLY | |
5 | VAL | GLU | MET | SER | ARG | ASP | LEU | ALA | TYR | ALA | |
6 | LYS | VAL | TYR | VAL | THR | PHE | LEU | ASN | ASP | LYS | |
7 | ASP | GLU | ASP | ALA | VAL | LYS | ALA | GLY | ILE | LYS | |
8 | ALA | LEU | GLN | GLU | ALA | SER | GLY | PHE | ILE | ARG | |
9 | SER | LEU | LEU | GLY | LYS | ALA | MET | ARG | LEU | ARG | |
10 | ILE | VAL | PRO | GLU | LEU | THR | PHE | PHE | TYR | ASP | |
11 | ASN | SER | LEU | VAL | GLU | GLY | MET | ARG | MET | SER | |
12 | ASN | LEU | VAL | THR | SER | VAL | VAL | LYS | HIS | ASP | |
13 | GLU | GLU | ARG | ARG | VAL | ASN | PRO | ASP | ASP | SER | |
14 | LYS | GLU | ASP | ALA | LEU | GLU | VAL | LEU | PHE | GLN |
Samples:
sample_1: RbfA, [U-98% 13C; U-98% 15N], 400 uM; HEPES 10 mM; MgCl2 6 mM; NH4Cl 30 mM; TCEP 75 uM
sample_conditions_1: ionic strength: 40 mM; pH: 7.6; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCAHA | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HNH NOESY | sample_1 | isotropic | sample_conditions_1 |
3D CNH NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CAHA | sample_1 | isotropic | sample_conditions_1 |
3D HCH NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
Xplor-NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
Sparky, Goddard - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE III 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts