BMRB Entry 25700
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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/BMR25700
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Title: Solution Structure of R. palustris CsgH PubMed: 27098162
Deposition date: 2015-07-13 Original release date: 2016-05-23
Authors: Hawthorne, William; Taylor, Jonathan; Escalera-Maurer, Andres; Lambert, Sebastian; Koch, Marion; Scull, Nicola; Sefer, Lea; Xu, Yinqi; Matthews, Steve
Citation: Taylor, Jonathan; Hawthorne, William; Fletcher, Catherine; Lo, Joanne; Koch, Marion; Darvill, Nicholas; Scull, Nicola; Escalera-Maurer, Andres; Sefer, Lea; Wenman, Rosemary; Lambert, Sebastian; Xu, Yinqi; Turner, Benjamin; Kazarian, Sergei; Bubeck, Doryen; de Simone, Alfonso; Knowles, Tuomas; Matthews, Steve. "Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones" Sci. Rep. 6, 24656-24656 (2016).
Assembly members:
CsgH, polymer, 106 residues, 10492.875 Da.
Natural source: Common Name: a-proteobacteria Taxonomy ID: 1076 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhodopseudomonas palustris
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CsgH: MVQCEVEAAVSGGHVTLQGV
ITAVRDGAGSYKLAVDKAGA
AGTSRIKQAGAFTAIAEQRV
TVGNVVLDYSSANRYAARLD
VSFGSVTIQCNLDPETVKLE
HHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 399 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 632 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 106 residues - 10492.875 Da.
Native N-terminal Sequence: MAVDQVPPV has been replaced with a single N-terminal Methionine.
| 1 | MET | VAL | GLN | CYS | GLU | VAL | GLU | ALA | ALA | VAL | ||||
| 2 | SER | GLY | GLY | HIS | VAL | THR | LEU | GLN | GLY | VAL | ||||
| 3 | ILE | THR | ALA | VAL | ARG | ASP | GLY | ALA | GLY | SER | ||||
| 4 | TYR | LYS | LEU | ALA | VAL | ASP | LYS | ALA | GLY | ALA | ||||
| 5 | ALA | GLY | THR | SER | ARG | ILE | LYS | GLN | ALA | GLY | ||||
| 6 | ALA | PHE | THR | ALA | ILE | ALA | GLU | GLN | ARG | VAL | ||||
| 7 | THR | VAL | GLY | ASN | VAL | VAL | LEU | ASP | TYR | SER | ||||
| 8 | SER | ALA | ASN | ARG | TYR | ALA | ALA | ARG | LEU | ASP | ||||
| 9 | VAL | SER | PHE | GLY | SER | VAL | THR | ILE | GLN | CYS | ||||
| 10 | ASN | LEU | ASP | PRO | GLU | THR | VAL | LYS | LEU | GLU | ||||
| 11 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: CsgH, [U-98% 13C; U-98% 15N], 400 uM; sodium chloride 150 mM; MES 10 mM; D2O, [U-2H], 10%; H2O 90%
sample_2: CsgH, [U-98% 13C; U-98% 15N], 400 uM; sodium chloride 150 mM; MES 10 mM; D2O, [U-2H], 100%
sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 292 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v2.3, Linge, O'Donoghue and Nilges - structure solution
NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment
CcpNmr v2.4.0, Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, Llinas M, Ulrich EL, Markley JL, Ionides J, Laue ED. - chemical shift assignment, peak picking
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Bruker Avance 950 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts