BMRB Entry 31031
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/BMR31031
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 Structure of Streptococcal Protein GB1 Backbone Modified Variant: beta-ACPC24, beta-3-Lys28, beta-3-Lys31, beta-ACPC35
Deposition date: 2022-06-29 Original release date: 2022-11-17
Authors: Rao, S.; Reinert, Z.
Citation: Rao, S.; Harmon, T.; Heath, S.; Wolfe, J.; Santhouse, J.; O'Brien, G.; Distefano, A.; Reinert, Z.; Horne, W.. "Chemical Shifts of Artificial Monomers Used to Construct Heterogeneous-Backbone Protein Mimetics in Random Coil and Folded States" to be published ., .-..
Assembly members:
entity_1, polymer, 57 residues, 6246.825 Da.
Natural source: Common Name: Streptococcus Taxonomy ID: 1301 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus not available
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: DTYKLILNGKTLKGETTTEA
VDAXTAEKVFKQYAXDNGVD
GEWTYDDATKTFTVTEX
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 388 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 57 residues - 6246.825 Da.
| 1 | ASP | THR | TYR | LYS | LEU | ILE | LEU | ASN | GLY | LYS | ||||
| 2 | THR | LEU | LYS | GLY | GLU | THR | THR | THR | GLU | ALA | ||||
| 3 | VAL | ASP | ALA | XCP | THR | ALA | GLU | B3K | VAL | PHE | ||||
| 4 | B3K | GLN | TYR | ALA | XCP | ASP | ASN | GLY | VAL | ASP | ||||
| 5 | GLY | GLU | TRP | THR | TYR | ASP | ASP | ALA | THR | LYS | ||||
| 6 | THR | PHE | THR | VAL | THR | GLU | NH2 |
Samples:
sample_1: Immunoglobulin G-binding protein G 0.65 mM; sodium phosphate 20 mM; DSS 0.1 mM
sample_conditions_1: ionic strength: 40 mM; pH: 7 pH*; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - processing
NMRFAM-SPARKY, Lee, Tonelli, Markley - data analysis
ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation
NMR spectrometers:
- Bruker AVANCE 700 MHz