BMRB Entry 16997
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16997
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Lemak, Alexander; Yee, Adelinda; Garcia, Maite; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution structure of protein SF1141 from Shigella flexneri 2a." .
Assembly members:
sf1141, polymer, 112 residues, 13259.014 Da.
Natural source: Common Name: Shigella flexneri Taxonomy ID: 42897 Superkingdom: Bacteria Kingdom: not available Genus/species: Shigella flexneri
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: p15Tv lic
Entity Sequences (FASTA):
sf1141: MNIGRLRDRITIQTLKQTRD
ITGEILETWEDGHTLWASVN
MVSSKEAISSGAELAIGTVR
IWIRYRKDINATSRIKVSTG
PLAGRVLNIIGQPLPDAART
RLEILCREGAEK
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 484 |
| 15N chemical shifts | 115 |
| 1H chemical shifts | 806 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SF1141 | 1 |
Entities:
Entity 1, SF1141 112 residues - 13259.014 Da.
| 1 | MET | ASN | ILE | GLY | ARG | LEU | ARG | ASP | ARG | ILE | ||||
| 2 | THR | ILE | GLN | THR | LEU | LYS | GLN | THR | ARG | ASP | ||||
| 3 | ILE | THR | GLY | GLU | ILE | LEU | GLU | THR | TRP | GLU | ||||
| 4 | ASP | GLY | HIS | THR | LEU | TRP | ALA | SER | VAL | ASN | ||||
| 5 | MET | VAL | SER | SER | LYS | GLU | ALA | ILE | SER | SER | ||||
| 6 | GLY | ALA | GLU | LEU | ALA | ILE | GLY | THR | VAL | ARG | ||||
| 7 | ILE | TRP | ILE | ARG | TYR | ARG | LYS | ASP | ILE | ASN | ||||
| 8 | ALA | THR | SER | ARG | ILE | LYS | VAL | SER | THR | GLY | ||||
| 9 | PRO | LEU | ALA | GLY | ARG | VAL | LEU | ASN | ILE | ILE | ||||
| 10 | GLY | GLN | PRO | LEU | PRO | ASP | ALA | ALA | ARG | THR | ||||
| 11 | ARG | LEU | GLU | ILE | LEU | CYS | ARG | GLU | GLY | ALA | ||||
| 12 | GLU | LYS |
Samples:
sample_1: sf1141, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 500 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 500 M; pH: 7.7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-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 |
| 3D 1H-13C_arom NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC (IPAP) | sample_1 | anisotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - peak picking
FMC, Lemak, Steren, Llinas, Arrowsmith - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| EMBL | CDK49410 CDX06441 CEP56120 CTS44973 CTS74968 |
| GB | AAN42758 AAP16648 ADA73539 AIL35230 AIL40152 |
| REF | NP_707051 WP_001020659 WP_001020661 WP_001020662 WP_001020663 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks