BMRB Entry 17615
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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/BMR17615
MolProbity Validation Chart
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Title: Solution Structure of RfaH carboxyterminal domain PubMed: 22817892
Deposition date: 2011-05-02 Original release date: 2012-07-30
Authors: Burmann, Bjoern; Schweimer, Kristian; Roesch, Paul
Citation: Burmann, Bjoern; Schweimer, Kristian; Roesch, Paul; Knauer, Stefan; Mooney, Rachel; Sevostyanova, Anastasia; Landick, Robert; Artsimovitch, Irina. "An alpha-helix to beta-barrel domain switch transforms the transcription factor RfaH into a translation factor" Cell 150, 291-303 (2012).
Assembly members:
entity, polymer, 66 residues, 7269.401 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: GAMGPKDIVDPATPYPGDKV
IITEGAFEGFQAIFTEPDGE
ARSMLLLNLINKEIKHSVKN
TEFRKL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 211 |
| 15N chemical shifts | 62 |
| 1H chemical shifts | 473 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RfaH | 1 |
Entities:
Entity 1, RfaH 66 residues - 7269.401 Da.
| 1 | GLY | ALA | MET | GLY | PRO | LYS | ASP | ILE | VAL | ASP | ||||
| 2 | PRO | ALA | THR | PRO | TYR | PRO | GLY | ASP | LYS | VAL | ||||
| 3 | ILE | ILE | THR | GLU | GLY | ALA | PHE | GLU | GLY | PHE | ||||
| 4 | GLN | ALA | ILE | PHE | THR | GLU | PRO | ASP | GLY | GLU | ||||
| 5 | ALA | ARG | SER | MET | LEU | LEU | LEU | ASN | LEU | ILE | ||||
| 6 | ASN | LYS | GLU | ILE | LYS | HIS | SER | VAL | LYS | ASN | ||||
| 7 | THR | GLU | PHE | ARG | LYS | LEU |
Samples:
sample_1: RfaH-CTD, [U-99% 13C; U-99% 15N], 0.5 mM; HEPES 0.025 mM; NaCl 0.05 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 75 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAB38193 BAE77461 BAG79652 BAI27905 BAI33028 |
| EMBL | CAA46147 CAP78305 CAQ34199 CAR00816 CAR05481 |
| GB | AAA67638 AAA91060 AAC76845 AAG10071 AAG59036 |
| REF | NP_312797 NP_418284 NP_709646 WP_001161073 WP_001192387 |
| SP | P0AFW0 P0AFW1 Q0TAL4 Q8FBI4 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts