BMRB Entry 16743
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16743
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Title: Three dimensional structure of HuPrP(90-231 M129 Q212P) PubMed: 20661422
Deposition date: 2010-02-23 Original release date: 2010-09-02
Authors: Ilc, Gregor; Giachin, Gabriele; Jaremko, Mariusz; Jaremko, Lukasz; Zhukov, Igor; Plavec, Janez; Legname, Guiseppe
Citation: Ilc, Gregor; Giachin, Gabriele; Jaremko, Mariusz; Jaremko, Lukasz; Benetti, Federico; Plavec, Janez; Zhukov, Igor; Legname, Guiseppe. "NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features" PLoS One 5, e11715-e11715 (2010).
Assembly members:
HuPrP(90-231 M129 Q212P), polymer, 148 residues, 16966.982 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):
HuPrP(90-231 M129 Q212P): GQGGGTHSQWNKPSKPKTNM
KHMAGAAAAGAVVGGLGGYM
LGSAMSRPIIHFGSDYEDRY
YRENMHRYPNQVYYRPMDEY
SNQNNFVHDCVNITIKQHTV
TTTTKGENFTETDVKMMERV
VEPMCITQYERESQAYYQRG
SSHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 610 |
| 15N chemical shifts | 147 |
| 1H chemical shifts | 942 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HuPrP(90-231 M129 Q212P) | 1 |
Entities:
Entity 1, HuPrP(90-231 M129 Q212P) 148 residues - 16966.982 Da.
His-Tag6 on C-terminus
| 1 | GLY | GLN | GLY | GLY | GLY | THR | HIS | SER | GLN | TRP | ||||
| 2 | ASN | LYS | PRO | SER | LYS | PRO | LYS | THR | ASN | MET | ||||
| 3 | LYS | HIS | MET | ALA | GLY | ALA | ALA | ALA | ALA | GLY | ||||
| 4 | ALA | VAL | VAL | GLY | GLY | LEU | GLY | GLY | TYR | MET | ||||
| 5 | LEU | GLY | SER | ALA | MET | SER | ARG | PRO | ILE | ILE | ||||
| 6 | HIS | PHE | GLY | SER | ASP | TYR | GLU | ASP | ARG | TYR | ||||
| 7 | TYR | ARG | GLU | ASN | MET | HIS | ARG | TYR | PRO | ASN | ||||
| 8 | GLN | VAL | TYR | TYR | ARG | PRO | MET | ASP | GLU | TYR | ||||
| 9 | SER | ASN | GLN | ASN | ASN | PHE | VAL | HIS | ASP | CYS | ||||
| 10 | VAL | ASN | ILE | THR | ILE | LYS | GLN | HIS | THR | VAL | ||||
| 11 | THR | THR | THR | THR | LYS | GLY | GLU | ASN | PHE | THR | ||||
| 12 | GLU | THR | ASP | VAL | LYS | MET | MET | GLU | ARG | VAL | ||||
| 13 | VAL | GLU | PRO | MET | CYS | ILE | THR | GLN | TYR | GLU | ||||
| 14 | ARG | GLU | SER | GLN | ALA | TYR | TYR | GLN | ARG | GLY | ||||
| 15 | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: PrP(Q212P), [U-98% 13C; U-98% 15N], 1.0 mM; H2O 90%; D2O 10%; NaCl 150 mM
sample_2: PrP(Q212P), [U-98% 13C; U-98% 15N], 1.0 mM; D2O 100%; NaCl 150 mM
sample_conditions_1: ionic strength: 150 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 150 mM; pH: 5.1; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_2 |
| 3D CCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Varian Uniform NMR System 800 MHz
- Varian Uniform NMR System 700 MHz
Related Database Links:
| BMRB | 15676 16757 17714 17756 17757 17780 18426 18550 19268 4379 4402 4434 4620 4641 4736 |
| PDB | |
| DBJ | BAA00011 BAF62360 BAG32276 BAG32277 BAG32278 |
| EMBL | CAA58442 CAG46836 CAG46869 |
| GB | AAA19664 AAA60182 AAA68632 AAA68633 AAB59442 |
| REF | NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592 |
| SP | P04156 P40252 P61766 P61767 P61768 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts