BMRB Entry 25508
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25508
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Title: 1H, 13C, and 15N Chemical Shift Assignments and structure of Probable Fe(2+)-trafficking protein from Burkholderia pseudomallei 1710b.
Deposition date: 2015-02-26 Original release date: 2015-03-23
Authors: Tang, Changyan; Yang, Fan; Barnwal, Ravi P; Barnwal, Gabriele
Citation: Tang, Changyan; Yang, Fan; Barnwal, Ravi P; Barnwal, Gabriele. "1H, 13C, and 15N Chemical Shift Assignments and structure of Probable Fe(2+)-trafficking protein from Burkholderia pseudomallei 1710b." To be Published ., .-..
Assembly members:
entity, polymer, 91 residues, 10388.955 Da.
Natural source: Common Name: b-proteobacteria Taxonomy ID: 320372 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia pseudomallei
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MARMIHCAKLGKEAEGLDFP
PLPGELGKRLYESVSKQAWQ
DWLKQQTMLINENRLNMADP
RARQYLMKQTEKYFFGEGAD
QASGYVPPAQG
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 492 |
| 13C chemical shifts | 361 |
| 15N chemical shifts | 93 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 91 residues - 10388.955 Da.
| 1 | MET | ALA | ARG | MET | ILE | HIS | CYS | ALA | LYS | LEU | ||||
| 2 | GLY | LYS | GLU | ALA | GLU | GLY | LEU | ASP | PHE | PRO | ||||
| 3 | PRO | LEU | PRO | GLY | GLU | LEU | GLY | LYS | ARG | LEU | ||||
| 4 | TYR | GLU | SER | VAL | SER | LYS | GLN | ALA | TRP | GLN | ||||
| 5 | ASP | TRP | LEU | LYS | GLN | GLN | THR | MET | LEU | ILE | ||||
| 6 | ASN | GLU | ASN | ARG | LEU | ASN | MET | ALA | ASP | PRO | ||||
| 7 | ARG | ALA | ARG | GLN | TYR | LEU | MET | LYS | GLN | THR | ||||
| 8 | GLU | LYS | TYR | PHE | PHE | GLY | GLU | GLY | ALA | ASP | ||||
| 9 | GLN | ALA | SER | GLY | TYR | VAL | PRO | PRO | ALA | GLN | ||||
| 10 | GLY |
Samples:
sample_1: Probable Fe(2+)-trafficking protein, [U-95% 13C; U-95% 15N], 1 mM; H2O 90%; H2O 10%
sample_conditions_1: temperature: 298 K; pH: 6.5; pressure: 1 atm
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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CCPNMR, CCPN - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution, refinement
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Bruker AMX 500 MHz
- Bruker Avance 800 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts