BMRB Entry 16184
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/BMR16184
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: Mouse Prion Protein (121-231) with Mutations Y225A and Y226A PubMed: 19393664
Deposition date: 2009-02-24 Original release date: 2009-05-20
Authors: Christen, Barbara; Hornemann, Simone; Damberger, Fred; Wuthrich, Kurt
Citation: Christen, Barbara; Hornemann, Simone; Damberger, Fred; Wuthrich, Kurt. "Prion Protein NMR Structure from Tammar Wallaby (Macropus eugenii) Shows that the beta2-alpha2 Loop Is Modulated by Long-Range Sequence Effects" J. Mol. Biol. ., .-. (2009).
Assembly members:
mpp_121-231, polymer, 114 residues, 13167.715 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
mpp_121-231: GSVVGGLGGYMLGSAMSRPM
IHFGNDWEDRYYRENMYRYP
NQVYYRPVDQYSNQNNFVHD
CVNITIKQHTVTTTTKGENF
TETDVKMMERVVEQMCVTQY
QKESQAAADGRRSS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 364 |
| 15N chemical shifts | 135 |
| 1H chemical shifts | 412 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | mpp_121-231 | 1 |
Entities:
Entity 1, mpp_121-231 114 residues - 13167.715 Da.
| 1 | GLY | SER | VAL | VAL | GLY | GLY | LEU | GLY | GLY | TYR | ||||
| 2 | MET | LEU | GLY | SER | ALA | MET | SER | ARG | PRO | MET | ||||
| 3 | ILE | HIS | PHE | GLY | ASN | ASP | TRP | GLU | ASP | ARG | ||||
| 4 | TYR | TYR | ARG | GLU | ASN | MET | TYR | ARG | TYR | PRO | ||||
| 5 | ASN | GLN | VAL | TYR | TYR | ARG | PRO | VAL | ASP | GLN | ||||
| 6 | TYR | SER | ASN | GLN | ASN | ASN | PHE | VAL | HIS | ASP | ||||
| 7 | CYS | VAL | ASN | ILE | THR | ILE | LYS | GLN | HIS | THR | ||||
| 8 | VAL | THR | THR | THR | THR | LYS | GLY | GLU | ASN | PHE | ||||
| 9 | THR | GLU | THR | ASP | VAL | LYS | MET | MET | GLU | ARG | ||||
| 10 | VAL | VAL | GLU | GLN | MET | CYS | VAL | THR | GLN | TYR | ||||
| 11 | GLN | LYS | GLU | SER | GLN | ALA | ALA | ALA | ASP | GLY | ||||
| 12 | ARG | ARG | SER | SER |
Samples:
sample_1: sodium acetate, [U-100% 2H], 10 mM; entity, [U-99% 13C; U-99% 15N], 2 mM
sample_conditions_1: ionic strength: 0.01 M; pH: 4.5; pressure: 1 atm; temperature: 293.1 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - data analysis
ATHNOS-CANDID v1.2, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking
DYANA v1.0.3, Guntert, Mumenthaler and Wuthrich - structure solution
OPALP, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
Molmol, Koradi, Billeter and Wuthrich - data analysis
xwinnmr, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker DRX 600 MHz
- Bruker DRX 750 MHz
- Bruker Avance 900 MHz