BMRB Entry 25226
Click here to enlarge.
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/BMR25226
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: Structure of the cis-(Tyr39-Pro40) form of the Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1)
Deposition date: 2014-09-15 Original release date: 2015-12-07
Authors: Paramonov, Alexander; Shenkarev, Zakhar; Lyukmanova, Ekaterina; Arseniev, Alexander
Citation: Lyukmanova, Ekaterina; Shenkarev, Zakhar; Shulepko, Mikhail; Paramonov, Alexander; Kudryavsev, Denis; Astapova, Maria; Tompsen, Morten; Kasheverov, Igor; Feofanov, Alexey; Arseniev, Alexander; Tsetlin, Vikor; Dolgikh, Dmitrii; Kirpichnikov, Mikhail. "Structural and Functional Properties of Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1) Imply a Non-Canonical Mode of Interaction with 7 nAChR" FEBS Lett. ., .-..
Assembly members:
Slurp1, polymer, 82 residues, 8992.387 Da.
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Slurp1: MLKCYTCKEPMTSASCRTIT
RCKPEDTACMTTLVTVEAEY
PFNQSPVVTRSCSSSCVATD
PDSIGAAHLIFCCFRDLCNS
EL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 247 |
| 15N chemical shifts | 82 |
| 1H chemical shifts | 535 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Slurp1 | 1 |
Entities:
Entity 1, Slurp1 82 residues - 8992.387 Da.
Non-native Methionine 100 is introduced due to recombinant production
| 1 | MET | LEU | LYS | CYS | TYR | THR | CYS | LYS | GLU | PRO | ||||
| 2 | MET | THR | SER | ALA | SER | CYS | ARG | THR | ILE | THR | ||||
| 3 | ARG | CYS | LYS | PRO | GLU | ASP | THR | ALA | CYS | MET | ||||
| 4 | THR | THR | LEU | VAL | THR | VAL | GLU | ALA | GLU | TYR | ||||
| 5 | PRO | PHE | ASN | GLN | SER | PRO | VAL | VAL | THR | ARG | ||||
| 6 | SER | CYS | SER | SER | SER | CYS | VAL | ALA | THR | ASP | ||||
| 7 | PRO | ASP | SER | ILE | GLY | ALA | ALA | HIS | LEU | ILE | ||||
| 8 | PHE | CYS | CYS | PHE | ARG | ASP | LEU | CYS | ASN | SER | ||||
| 9 | GLU | LEU |
Samples:
sample_1: Slurp1, [U-100% 15N], 0.3 mM; H20 95%; D20 5%
sample_2: Slurp1, [U-100% 13C; U-100% 15N], 0.3 mM; H20 95%; D20 5%
sample_3: Slurp1, [U-100% 13C; U-100% 15N], 0.3 mM; D20 100%
sample_conditions_1: ionic strength: 0.001 M; pH: 4.7; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.0, Bruker Biospin - collection, processing
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
CARA v1.8, Keller R. - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
- 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