BMRB Entry 30925
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30925
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: NMR Solution structure of Se0862 PubMed: 34559429
Deposition date: 2021-06-11 Original release date: 2021-07-12
Authors: Zhang, N.; LiWang, A.
Citation: Huang, Yuanpeng Janet; Zhang, Ning; Bersch, Beate; Fidelis, Krzysztof; Inouye, Masayori; Ishida, Yojiro; Kryshtafovych, Andriy; Kobayashi, Naohiro; Kuroda, Yutaka; Liu, Gaohua; LiWang, Andy; Swapna, G; Wu, Nan; Yamazaki, Toshio; Montelione, Gaetano. "Assessment of prediction methods for protein structures determined by NMR in CASP14: Impact of AlphaFold2" Proteins 89, 1959-1976 (2021).
Assembly members:
entity_1, polymer, 125 residues, 14425.336 Da.
Natural source: Common Name: Synechococcus elongatus Taxonomy ID: 32046 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
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 461 |
| 15N chemical shifts | 121 |
| 1H chemical shifts | 791 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_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: Se0862, [U-100% 13C; U-100% 15N], 0.6 mM; TRIS 20 mM; sodium chloride 100 mM; TCEP 5 mM; DSS 10 uM; sodium azide 0.02 % v/v
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 HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker AVANCE DMX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts