BMRB Entry 17321
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17321
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Title: New high resolution NMR structure of gpW (W protein of bacteriophage lambda) at neutral pH PubMed: 22087227
Deposition date: 2010-11-24 Original release date: 2011-11-07
Authors: Sborgi, Lorenzo; Verma, Abhinav; Munoz, Victor; de Alba, Eva
Citation: Sborgi, Lorenzo; Verma, Abhinav; Munoz, Victor; de Alba, Eva. "Revisiting the NMR structure of the ultrafast downhill folding protein gpW from bacteriophage ." PLoS ONE 6, e26409-e26409 (2011).
Assembly members:
gpW, polymer, 62 residues, 6989.108 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):
gpW: MVRQEELAAARAALHDLMTG
KRVATVQKDGRRVEFTATSV
SDLKKYIAELEVQTGMTQRR
RG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 203 |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 423 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | W protein of bacteriophage lambda | 1 |
Entities:
Entity 1, W protein of bacteriophage lambda 62 residues - 6989.108 Da.
| 1 | MET | VAL | ARG | GLN | GLU | GLU | LEU | ALA | ALA | ALA | ||||
| 2 | ARG | ALA | ALA | LEU | HIS | ASP | LEU | MET | THR | GLY | ||||
| 3 | LYS | ARG | VAL | ALA | THR | VAL | GLN | LYS | ASP | GLY | ||||
| 4 | ARG | ARG | VAL | GLU | PHE | THR | ALA | THR | SER | VAL | ||||
| 5 | SER | ASP | LEU | LYS | LYS | TYR | ILE | ALA | GLU | LEU | ||||
| 6 | GLU | VAL | GLN | THR | GLY | MET | THR | GLN | ARG | ARG | ||||
| 7 | ARG | GLY |
Samples:
sample_1: gpW, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%; phosphate buffer 20 mM
sample_2: gpW, [U-13C; U-15N], 1 mM; D2O 100%; phosphate buffer 20 mM
sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 294 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 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | 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 |
| 4D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing
PIPP, Garrett - chemical shift assignment, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 17322 |
| PDB | |
| DBJ | BAG76119 BAG77589 BAI23937 BAI29406 GAL55727 |
| EMBL | CAP75664 CAQ31249 CAQ97648 CAQ98444 CAR11829 |
| GB | AAA96535 AAG55981 AAN81624 AAZ89070 ABG69179 |
| REF | NP_040582 WP_000198149 WP_000246867 WP_001571330 WP_001657975 |
| SP | P68659 P68660 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts