BMRB Entry 19550
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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/BMR19550
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Title: Domain 1 of E. coli ribosomal protein S1 PubMed: 24682851
Deposition date: 2013-10-11 Original release date: 2014-04-14
Authors: GIRAUD, Pierre; CRECHET, Jean-Bernard; BONTEMS, Francois; UZAN, Marc; SIZUN, Christina
Citation: Giraud, Pierre; Crechet, Jean-Bernard; Uzan, Marc; Bontems, Francois; Sizun, Christina. "Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1." Biomol. NMR Assignments ., .-. (2014).
Assembly members:
S1F1, polymer, 96 residues, 10408.6085 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):
S1F1: GIDPFTESLKEIETRPGSIV
RGVVVAIDKDVVLVDAGLKS
ESAIPAEQFKNAQGELEIQV
GDEVDVALDAVEDGFGETLL
SREKAKRHEAWITLEK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 389 |
| 15N chemical shifts | 95 |
| 1H chemical shifts | 659 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | S1F1 | 1 |
Entities:
Entity 1, S1F1 96 residues - 10408.6085 Da.
The six first residues are generated by TOPO cloning and TEV cleavage.
| 1 | GLY | ILE | ASP | PRO | PHE | THR | GLU | SER | LEU | LYS | ||||
| 2 | GLU | ILE | GLU | THR | ARG | PRO | GLY | SER | ILE | VAL | ||||
| 3 | ARG | GLY | VAL | VAL | VAL | ALA | ILE | ASP | LYS | ASP | ||||
| 4 | VAL | VAL | LEU | VAL | ASP | ALA | GLY | LEU | LYS | SER | ||||
| 5 | GLU | SER | ALA | ILE | PRO | ALA | GLU | GLN | PHE | LYS | ||||
| 6 | ASN | ALA | GLN | GLY | GLU | LEU | GLU | ILE | GLN | VAL | ||||
| 7 | GLY | ASP | GLU | VAL | ASP | VAL | ALA | LEU | ASP | ALA | ||||
| 8 | VAL | GLU | ASP | GLY | PHE | GLY | GLU | THR | LEU | LEU | ||||
| 9 | SER | ARG | GLU | LYS | ALA | LYS | ARG | HIS | GLU | ALA | ||||
| 10 | TRP | ILE | THR | LEU | GLU | LYS |
Samples:
S1F1-15N13C-H2O: S1F1, [U-99% 13C; U-99% 15N], 0.2 ± 2e-05 mM; potassium phosphate 25.0 ± 0.0025 mM; potassium chloride 200.0 ± 0.0025 mM; H2O 93%; D2O, [U-100% 2H], 7%
S1F1-15N13C-D2O: S1F1, [U-99% 13C; U-99% 15N], 0.2 ± 2e-05 mM; potassium phosphate 25.0 ± 0.0025 mM; potassium chloride 200.0 ± 0.0025 mM; D2O, [U-100% 2H], 100%
S1F1-15N: S1F1, [U-99% 13C; U-99% 15N], 0.5 ± 2e-05 mM; potassium phosphate 25.0 ± 0.0025 mM; potassium chloride 200.0 ± 0.0025 mM; H2O 93%; D2O, [U-100% 2H], 7%
Condition_1: ionic strength: 0.200 M; pH: 6.500; pressure: 1.000 atm; temperature: 293.000 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | S1F1-15N13C-H2O | isotropic | Condition_1 |
| 3D HNCA | S1F1-15N13C-H2O | isotropic | Condition_1 |
| 3D HN(CO)CA | S1F1-15N13C-H2O | isotropic | Condition_1 |
| 3D HNCACB | S1F1-15N13C-H2O | isotropic | Condition_1 |
| 3D HCCH-TOCSY | S1F1-15N13C-D2O | isotropic | Condition_1 |
| 3D HNCO | S1F1-15N13C-H2O | isotropic | Condition_1 |
| 3D HN(CA)CO | S1F1-15N13C-H2O | isotropic | Condition_1 |
| 3D 1H-15N NOESY | S1F1-15N | isotropic | Condition_1 |
| 3D 1H-13C NOESY | S1F1-15N13C-D2O | isotropic | Condition_1 |
| 2D 1H-13C HSQC | S1F1-15N13C-D2O | isotropic | Condition_1 |
| 3D CCH-TOCSY | S1F1-15N13C-D2O | isotropic | Condition_1 |
| 3D HCCH-TOCSY aromatic | S1F1-15N13C-D2O | isotropic | Condition_1 |
| 2D 1H-1H NOESY | S1F1-15N13C-D2O | isotropic | Condition_1 |
Software:
CCPNmr ANALYSIS v2.2, CCPN - Spectrum analysis, Spectrum display
TOPSPIN v3.1, Bruker, Guntert, Mumenthaler and Wuthrich - Spectrum processing, Structure calculation
NMRPipe vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectrum processing
TALOS+ vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Dihedral angles
NMR spectrometers:
- Bruker Avance 950 MHz
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| UniProt | P0AG67 |
| BMRB | 19554 |
| PDB | |
| DBJ | BAA35655 BAB34417 BAG76494 BAH62634 BAI24353 |
| EMBL | CAA23630 CAA23644 CAD05381 CAP75381 CAQ31439 |
| GB | AAC73997 AAG55396 AAL19915 AAN42537 AAN79519 |
| PIR | AC0614 |
| PRF | 0804233A |
| REF | NP_309021 NP_415431 NP_455468 NP_459956 NP_706830 |
| SP | P0AG67 P0AG68 P0AG69 P0AG70 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts