BMRB Entry 30676
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30676
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Title: NMR structure of biofilm-related EbsA from Synechococcus elongatus PubMed: 32949024
Deposition date: 2019-09-23 Original release date: 2020-09-28
Authors: Zhang, N.; LiWang, A.
Citation: Zhang, N.; Chang, Y.; Tseng, R.; Ovchinnikov, S.; Schwarz, R.; LiWang, A.. "Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation." Protein Sci. 29, 2274-2280 (2020).
Assembly members:
entity_1, polymer, 125 residues, 14425.336 Da.
Natural source: Common Name: Synechococcus elongatus Taxonomy ID: 1140 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechococcus elongatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
Entity Sequences (FASTA):
entity_1: MRIDELVPADPRAVSLYTPY
YSQANRRRYLPYALSLYQGS
SIEGSRAVEGGAPISFVATW
TVTPLPADMTRCHLQFNNDA
ELTYEILLPNHEFLEYLIDM
LMGYQRMQKTDFPGAFYRRL
LGYDS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 461 |
| 15N chemical shifts | 121 |
| 1H chemical shifts | 794 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 125 residues - 14425.336 Da.
| 1 | MET | ARG | ILE | ASP | GLU | LEU | VAL | PRO | ALA | ASP | ||||
| 2 | PRO | ARG | ALA | VAL | SER | LEU | TYR | THR | PRO | TYR | ||||
| 3 | TYR | SER | GLN | ALA | ASN | ARG | ARG | ARG | TYR | LEU | ||||
| 4 | PRO | TYR | ALA | LEU | SER | LEU | TYR | GLN | GLY | SER | ||||
| 5 | SER | ILE | GLU | GLY | SER | ARG | ALA | VAL | GLU | GLY | ||||
| 6 | GLY | ALA | PRO | ILE | SER | PHE | VAL | ALA | THR | TRP | ||||
| 7 | THR | VAL | THR | PRO | LEU | PRO | ALA | ASP | MET | THR | ||||
| 8 | ARG | CYS | HIS | LEU | GLN | PHE | ASN | ASN | ASP | ALA | ||||
| 9 | GLU | LEU | THR | TYR | GLU | ILE | LEU | LEU | PRO | ASN | ||||
| 10 | HIS | GLU | PHE | LEU | GLU | TYR | LEU | ILE | ASP | MET | ||||
| 11 | LEU | MET | GLY | TYR | GLN | ARG | MET | GLN | LYS | THR | ||||
| 12 | ASP | PHE | PRO | GLY | ALA | PHE | TYR | ARG | ARG | LEU | ||||
| 13 | LEU | GLY | TYR | ASP | SER |
Samples:
sample_1: EbsA, [U-99% 13C; U-99% 15N], 0.6 mM
sample_conditions_1: ionic strength: 125 mM; pH: 7; pressure: 1013.25 mbar; temperature: 295 K
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 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D IPAP-HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CDCGCE)HE | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CDCG)HG | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 4D 13C-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.51, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMRFAM-SPARKY v1.414, Woonghee Lee, Marco Tonelli, and John L. Markley - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts