BMRB Entry 25966
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/BMR25966
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of C-terminal extramembrane domain of SH protein PubMed: 25100835
Deposition date: 2016-01-26 Original release date: 2016-02-15
Authors: Li, Yan; To, Janet; Surya, Wahyu; Torres, Jaume
Citation: Li, Yan; To, Janet; Verdia-Baguena, Carmina; Dossena, Silvia; Surya, Wahyu; Huang, Mei; Paulmichl, Markus; Liu, Ding Xiang; Aguilella, Vicente M; Torres, Jaume. "Inhibition of the Human Respiratory Syncytial Virus Small Hydrophobic Protein and Structural Variations in a Bicelle Environment" J Virol. 88, 11899-11914 (2014).
Assembly members:
entity, polymer, 27 residues, 3209.771 Da.
Natural source: Common Name: Human respiratory syncytial virus Taxonomy ID: 11250 Superkingdom: Viruses Kingdom: not available Genus/species: Pneumovirus not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: IAILNKLCEYNVFHNKTFEL
PRARVNT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 112 |
| 15N chemical shifts | 29 |
| 1H chemical shifts | 190 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 27 residues - 3209.771 Da.
| 1 | ILE | ALA | ILE | LEU | ASN | LYS | LEU | CYS | GLU | TYR | ||||
| 2 | ASN | VAL | PHE | HIS | ASN | LYS | THR | PHE | GLU | LEU | ||||
| 3 | PRO | ARG | ALA | ARG | VAL | ASN | THR |
Samples:
sample_1: entity, [U-13C; U-15N], 0.7 mM; DHPC-DLPC 9.5%; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 70 mM; pH: 5.5; pressure: 1 atm; temperature: 313 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Bruker Biospin, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, processing, structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts