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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/BMR16183
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
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. 389, 833-845 (2009).
PubMed: 19393664
Assembly members:
wpp_121-230, polymer, 112 residues, 13167.715 Da.
Natural source: Common Name: tammar wallaby Taxonomy ID: 9315 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Macropus Eugenii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pRSETA
Entity Sequences (FASTA):
wpp_121-230: GSVVGGLGGYMLGSAMSRPV
MHFGNEYEDRYYRENQYRYP
NQVMYRPIDQYGSQNSFVHD
CVNITVKQHTTTTTTKGENF
TETDIKIMERVVEQMCITQY
QNEYQAAQRYYN
Data type | Count |
13C chemical shifts | 473 |
15N chemical shifts | 132 |
1H chemical shifts | 782 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | wpp_121-230 | 1 |
Entity 1, wpp_121-230 112 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 | VAL | ||||
3 | MET | HIS | PHE | GLY | ASN | GLU | TYR | GLU | ASP | ARG | ||||
4 | TYR | TYR | ARG | GLU | ASN | GLN | TYR | ARG | TYR | PRO | ||||
5 | ASN | GLN | VAL | MET | TYR | ARG | PRO | ILE | ASP | GLN | ||||
6 | TYR | GLY | SER | GLN | ASN | SER | PHE | VAL | HIS | ASP | ||||
7 | CYS | VAL | ASN | ILE | THR | VAL | LYS | GLN | HIS | THR | ||||
8 | THR | THR | THR | THR | THR | LYS | GLY | GLU | ASN | PHE | ||||
9 | THR | GLU | THR | ASP | ILE | LYS | ILE | MET | GLU | ARG | ||||
10 | VAL | VAL | GLU | GLN | MET | CYS | ILE | THR | GLN | TYR | ||||
11 | GLN | ASN | GLU | TYR | GLN | ALA | ALA | GLN | ARG | TYR | ||||
12 | TYR | ASN |
sample_1: sodium acetate, [U-100% 2H], 10 mM; entity, [U-99% 13C; U-99% 15N], 1.5 mM; sodium azide 0.02%
sample_conditions_1: ionic strength: 0.01 M; pH: 4.5; pressure: 1 atm; temperature: 293.1 K
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 HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D H(CCCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D (H)C(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
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
TOPSPIN, Bruker Biospin - collection, processing
Download HSQC peak lists in one of the following formats:
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