Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19760
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Citation: Bryant, Jack Alfred; Morris, Faye; Knowles, Timothy; Maderbocus, Riyaz; Heinz, Eva; Boelter, Gabriela; Alodaini, Dema; Colyer, Adam; Wotherspoon, Peter; Staunton, Kara; Jeeves, Mark; Browning, Douglas; Sevastsyanovich, Yanina; Wells, Timothy; Rossiter, Amanda; Bavro, Vassiliy; Sridhar, Pooja; Ward, Douglas; Chong, Zhi-Soon; Goodall, Emily Ca; Icke, Christopher; Teo, Alvin Ck; Chng, Shu-Sin; Roper, David; Lithgow, Trevor; Cunningham, Adam; Banzhaf, Manuel; Overduin, Michael; Henderson, Ian. "Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation" Elife 9, .-. (2020).
PubMed: 33315009
Assembly members:
PlpA, polymer, 182 residues, 18772.311 Da.
Natural source: Common Name: enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET26b
Data type | Count |
13C chemical shifts | 686 |
15N chemical shifts | 172 |
1H chemical shifts | 1023 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity | 1 |
Entity 1, entity 182 residues - 18772.311 Da.
Residue 20 - represents non-native sequence. Replacement of Val with Ile due to cloning Residues 192-195 - Non-native due to cloning strategy Residues 196-201 - Non native - His Tag
1 | ILE | ALA | ALA | ALA | VAL | VAL | GLY | THR | ALA | ALA | ||||
2 | VAL | GLY | THR | LYS | ALA | ALA | THR | ASP | PRO | ARG | ||||
3 | SER | VAL | GLY | THR | GLN | VAL | ASP | ASP | GLY | THR | ||||
4 | LEU | GLU | VAL | ARG | VAL | ASN | SER | ALA | LEU | SER | ||||
5 | LYS | ASP | GLU | GLN | ILE | LYS | LYS | GLU | ALA | ARG | ||||
6 | ILE | ASN | VAL | THR | ALA | TYR | GLN | GLY | LYS | VAL | ||||
7 | LEU | LEU | VAL | GLY | GLN | SER | PRO | ASN | ALA | GLU | ||||
8 | LEU | SER | ALA | ARG | ALA | LYS | GLN | ILE | ALA | MET | ||||
9 | GLY | VAL | ASP | GLY | ALA | ASN | GLU | VAL | TYR | ASN | ||||
10 | GLU | ILE | ARG | GLN | GLY | GLN | PRO | ILE | GLY | LEU | ||||
11 | GLY | GLU | ALA | SER | ASN | ASP | THR | TRP | ILE | THR | ||||
12 | THR | LYS | VAL | ARG | SER | GLN | LEU | LEU | THR | SER | ||||
13 | ASP | LEU | VAL | LYS | SER | SER | ASN | VAL | LYS | VAL | ||||
14 | THR | THR | GLU | ASN | GLY | GLU | VAL | PHE | LEU | MET | ||||
15 | GLY | LEU | VAL | THR | GLU | ARG | GLU | ALA | LYS | ALA | ||||
16 | ALA | ALA | ASP | ILE | ALA | SER | ARG | VAL | SER | GLY | ||||
17 | VAL | LYS | ARG | VAL | THR | THR | ALA | PHE | THR | PHE | ||||
18 | ILE | LYS | GLY | GLY | LEU | GLU | HIS | HIS | HIS | HIS | ||||
19 | HIS | HIS |
sample_1: PlpA, [U-98% 13C; U-98% 15N], 1.5 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 6; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D H(C)CH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY-HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY-HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
H(C)CONH | sample_1 | isotropic | sample_conditions_1 |
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
ARIA v2.3, Linge, O'Donoghue and Nilges - refinement
SPARKY, Goddard - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
ProcheckNMR, Laskowski and MacArthur - refinement
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks