BMRB Entry 15642
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15642
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Title: Solution structure of the aminoterminal domain of E. coli NusG PubMed: 19500594
Deposition date: 2008-01-25 Original release date: 2009-06-10
Authors: Schweimer, Kristian; Scheckenhofer, Ulrich; Roesch, Paul
Citation: Mooney, Rachel Anne; Schweimer, Kristian; Roesch, Paul; Gottesman, Max; Landick, Robert. "Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators." J. Mol. Biol. 391, 341-358 (2009).
Assembly members:
NusG, polymer, 123 residues, 14096.366 Da.
Natural source: Common Name: not available 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):
NusG: MSEAPKKRWYVVQAFSGFEG
RVATSLREHIKLHNMEDLFG
EVMVPTEEVVEIRGGQRRKS
ERKFFPGYVLVQMVMNDASW
HLVRSVPRVMGFIGGTSDRP
APISDKEVDAIMNRLQQVGD
KPR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 498 |
| 15N chemical shifts | 122 |
| 1H chemical shifts | 790 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NusG | 1 |
Entities:
Entity 1, NusG 123 residues - 14096.366 Da.
| 1 | MET | SER | GLU | ALA | PRO | LYS | LYS | ARG | TRP | TYR | ||||
| 2 | VAL | VAL | GLN | ALA | PHE | SER | GLY | PHE | GLU | GLY | ||||
| 3 | ARG | VAL | ALA | THR | SER | LEU | ARG | GLU | HIS | ILE | ||||
| 4 | LYS | LEU | HIS | ASN | MET | GLU | ASP | LEU | PHE | GLY | ||||
| 5 | GLU | VAL | MET | VAL | PRO | THR | GLU | GLU | VAL | VAL | ||||
| 6 | GLU | ILE | ARG | GLY | GLY | GLN | ARG | ARG | LYS | SER | ||||
| 7 | GLU | ARG | LYS | PHE | PHE | PRO | GLY | TYR | VAL | LEU | ||||
| 8 | VAL | GLN | MET | VAL | MET | ASN | ASP | ALA | SER | TRP | ||||
| 9 | HIS | LEU | VAL | ARG | SER | VAL | PRO | ARG | VAL | MET | ||||
| 10 | GLY | PHE | ILE | GLY | GLY | THR | SER | ASP | ARG | PRO | ||||
| 11 | ALA | PRO | ILE | SER | ASP | LYS | GLU | VAL | ASP | ALA | ||||
| 12 | ILE | MET | ASN | ARG | LEU | GLN | GLN | VAL | GLY | ASP | ||||
| 13 | LYS | PRO | ARG |
Samples:
sample_1: entity, [U-98% 13C; U-98% 15N], 0.4 mM; potassium phosphate 10 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 10%; H2O 90%
sample_conditions_1: pH: 6.4; 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 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 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:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
Related Database Links:
| BMRB | 15490 |
| PDB | |
| DBJ | BAB38328 BAE73404 BAE77338 BAG79793 BAH61119 |
| EMBL | CAD09492 CAG73137 CAH19518 CAL10413 CAL22339 |
| GB | AAA24622 AAC43080 AAC76956 AAF33495 AAG59178 |
| PIR | AB0934 |
| REF | NP_312932 NP_418409 NP_457922 NP_463017 NP_709777 |
| SP | P0AA01 P0AA02 P0AA03 P0AFG0 P0AFG1 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts