BMRB Entry 25642
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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/BMR25642
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Title: Atomic structure of the cytoskeletal bactofilin BacA revealed by solid-state NMR PubMed: 26665178
Deposition date: 2015-05-29 Original release date: 2015-12-14
Authors: Shi, Chaowei; Fricke, Pascal; Lin, Lin; Chevelkov, Veniamin; Wegstroth, Melanie; Becker, Stefan; Thanbichler, Martin; Lange, Adam
Citation: Shi, Chaowei; Fricke, Pascal; Lin, Lin; Chevelkov, Veniamin; Wegstroth, Melanie; Becker, Stefan; Thanbichler, Martin; Lange, Adam. "Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR" Sci. Adv. 1, e1501087-e1501087 (2015).
Assembly members:
sample_uni, polymer, 184 residues, 10938.355 Da.
Natural source: Common Name: a-proteobacteria Taxonomy ID: 155892 Superkingdom: Bacteria Kingdom: not available Genus/species: Caulobacter crescentus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
sample_uni: MFSKQAKSNNKAPARIEPLP
TPMAATPAEPARRAPPKVAS
LLSADLTIEGGVTGEGELQI
DGVVKGDVRVGRLTVGETGH
VEGSVYAEAVEVRGRVVGAI
TSKQVRLYGTSYVDGDITHE
QLAMETGAFFQGRSLKFQRP
APAPSQPAPHPEHLAIAKSA
GGAPENSSSVDKLAAALEHH
HHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 418 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 97 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 184 residues - 10938.355 Da.
| 1 | MET | PHE | SER | LYS | GLN | ALA | LYS | SER | ASN | ASN | ||||
| 2 | LYS | ALA | PRO | ALA | ARG | ILE | GLU | PRO | LEU | PRO | ||||
| 3 | THR | PRO | MET | ALA | ALA | THR | PRO | ALA | GLU | PRO | ||||
| 4 | ALA | ARG | ARG | ALA | PRO | PRO | LYS | VAL | ALA | SER | ||||
| 5 | LEU | LEU | SER | ALA | ASP | LEU | THR | ILE | GLU | GLY | ||||
| 6 | GLY | VAL | THR | GLY | GLU | GLY | GLU | LEU | GLN | ILE | ||||
| 7 | ASP | GLY | VAL | VAL | LYS | GLY | ASP | VAL | ARG | VAL | ||||
| 8 | GLY | ARG | LEU | THR | VAL | GLY | GLU | THR | GLY | HIS | ||||
| 9 | VAL | GLU | GLY | SER | VAL | TYR | ALA | GLU | ALA | VAL | ||||
| 10 | GLU | VAL | ARG | GLY | ARG | VAL | VAL | GLY | ALA | ILE | ||||
| 11 | THR | SER | LYS | GLN | VAL | ARG | LEU | TYR | GLY | THR | ||||
| 12 | SER | TYR | VAL | ASP | GLY | ASP | ILE | THR | HIS | GLU | ||||
| 13 | GLN | LEU | ALA | MET | GLU | THR | GLY | ALA | PHE | PHE | ||||
| 14 | GLN | GLY | ARG | SER | LEU | LYS | PHE | GLN | ARG | PRO | ||||
| 15 | ALA | PRO | ALA | PRO | SER | GLN | PRO | ALA | PRO | HIS | ||||
| 16 | PRO | GLU | HIS | LEU | ALA | ILE | ALA | LYS | SER | ALA | ||||
| 17 | GLY | GLY | ALA | PRO | GLU | ASN | SER | SER | SER | VAL | ||||
| 18 | ASP | LYS | LEU | ALA | ALA | ALA | LEU | GLU | HIS | HIS | ||||
| 19 | HIS | HIS | HIS | HIS |
Samples:
sample_uni: sample_uni, [U-100% 13C; U-100% 15N], 95%; TRIS 20 mM; H2O 3%; DSS 0.1%
sample_2gly: sample_uni, [2- 13C] Glycerol, 95%; TRIS 20 mM; H2O 3%; DSS 0.1%
sample_13gly: sample_uni, [1,3- 13C] Glycerol, 95%; TRIS 20 mM; H2O 3%; DSS 0.1%
sample_deu: sample_deu, [U-100% 13C; U-100% 15N; U-100% 2H], 95%; TRIS 50 mM; H2O 3%; DSS 0.1%; EDTA 0.5 mM; DTT 1 mM
sample_conditions_1: ionic strength: 20 mM; pH: 7.5; pressure: 1 atm; temperature: 277 K
sample_conditions_2: ionic strength: 50 mM; pH: 8; pressure: 1 atm; temperature: 301 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| PDSD | sample_uni | solid | sample_conditions_1 |
| 3D NCACX | sample_uni | solid | sample_conditions_1 |
| 3D NCOCX | sample_uni | solid | sample_conditions_1 |
| 3D NCOCA | sample_uni | solid | sample_conditions_1 |
| 3D NCACO | sample_uni | solid | sample_conditions_1 |
| PDSD | sample_2gly | solid | sample_conditions_1 |
| PDSD | sample_2gly | solid | sample_conditions_1 |
| PDSD | sample_13gly | solid | sample_conditions_1 |
| PDSD | sample_13gly | solid | sample_conditions_1 |
| 2D NHHC | sample_13gly | solid | sample_conditions_1 |
| 3D (H)CANH | sample_deu | solid | sample_conditions_2 |
| 3D (H)CONH | sample_deu | solid | sample_conditions_2 |
| 3D (H)CACO(N)H | sample_deu | solid | sample_conditions_2 |
| 3D (H)COCA(N)H | sample_deu | solid | sample_conditions_2 |
| 3D (H)CA(CO)NH | sample_deu | solid | sample_conditions_2 |
| 4D HN(H)(H)NH | sample_deu | solid | sample_conditions_2 |
Software:
SPARKY v3.114, Goddard - chemical shift assignment, chemical shift calculation, peak picking
CCPN v2.4, CCPN - chemical shift assignment, chemical shift calculation, peak picking
TOPSPIN, Bruker Biospin - chemical shift calculation, collection, processing
X-PLOR_NIH v2.37, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, refinement, structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
- Bruker Avance 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts