BMRB Entry 34010
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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/BMR34010
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Title: S-nitrosylated 3D NMR structure of the cytoplasmic rhodanese domain of the inner membrane protein YgaP from Escherichia coli PubMed: 27473602
Deposition date: 2016-06-14 Original release date: 2016-08-15
Authors: Eichmann, C.; Tzitzilonis, C.; Nakamura, T.; Maslennikov, I.; Kwiatkowski, W.; Choe, S.; Lipton, S.; Guntert, P.; Riek, R.
Citation: Eichmann, C.; Tzitzilonis, C.; Nakamura, T.; Kwiatkowski, W.; Maslennikov, I.; Choe, S.; Lipton, S.; Riek, R.. "S-Nitrosylation Induces Structural and Dynamical Changes in a Rhodanese Family Protein." J. Mol. Biol. 428, 3737-3751 (2016).
Assembly members:
entity_1, polymer, 108 residues, 11716.311 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 BL21(DE3)
Entity Sequences (FASTA):
entity_1: ALTTISPHDAQELIARGAKL
IDIRDADEYLREHIPEADLA
PLSVLEQSGLPAKLRHEQII
FHCQAGKRTSNNADKLAAIA
APAEIFLLEDGIDGWKKAGL
PVAVNKSQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 310 |
| 1H chemical shifts | 654 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 108 residues - 11716.311 Da.
| 1 | ALA | LEU | THR | THR | ILE | SER | PRO | HIS | ASP | ALA | ||||
| 2 | GLN | GLU | LEU | ILE | ALA | ARG | GLY | ALA | LYS | LEU | ||||
| 3 | ILE | ASP | ILE | ARG | ASP | ALA | ASP | GLU | TYR | LEU | ||||
| 4 | ARG | GLU | HIS | ILE | PRO | GLU | ALA | ASP | LEU | ALA | ||||
| 5 | PRO | LEU | SER | VAL | LEU | GLU | GLN | SER | GLY | LEU | ||||
| 6 | PRO | ALA | LYS | LEU | ARG | HIS | GLU | GLN | ILE | ILE | ||||
| 7 | PHE | HIS | CYS | GLN | ALA | GLY | LYS | ARG | THR | SER | ||||
| 8 | ASN | ASN | ALA | ASP | LYS | LEU | ALA | ALA | ILE | ALA | ||||
| 9 | ALA | PRO | ALA | GLU | ILE | PHE | LEU | LEU | GLU | ASP | ||||
| 10 | GLY | ILE | ASP | GLY | TRP | LYS | LYS | ALA | GLY | LEU | ||||
| 11 | PRO | VAL | ALA | VAL | ASN | LYS | SER | GLN |
Samples:
sample_1: S-nitrosylated rhodanese domain, [U-99% 13C; U-99% 15N], 1 mM
sample_conditions_1: ionic strength: 0 mM; pH: 7; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 2D TROSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
OPAL v3.97, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
XEASY, Bartels et al. - chemical shift assignment
NMR spectrometers:
- Bruker AvanceIII 700 MHz