Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50845
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Citation: Toerner, Ricarda; Henot, Faustine; Awad, Rida; Macek, Pavel; Gans, Pierre; Boisbouvier, Jerome. "Backbone and methyl resonances assignment of the 87 kDa prefoldin from Pyrococcus horikoshii" Biomol. NMR Assignments 15, 351-360 (2021).
PubMed: 33988824
Assembly members:
entity_1, polymer, 117 residues, Formula weight is not available
entity_2, polymer, 148 residues, Formula weight is not available
Natural source: Common Name: Pyrococcus hirokoshii Taxonomy ID: 53953 Superkingdom: Archaea Kingdom: not available Genus/species: Pyrococcus hirokoshii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET23c
Entity Sequences (FASTA):
entity_1: MQNIPPQVQAMLGQLDTYQQ
QLQLVIQQKQKVQADLNEAK
KALEEIETLPDDAQIYKTVG
TLIVKTTKEKAVQELKEKIE
TLEVRLNALNRQEQKINEKV
KELTQKIQAALRPPTAG
entity_2: MAQNNKELEKLAYEYQVLQA
QAQILAQNLELLNLAKAEVQ
TVRETLENLKKIEEEKPEIL
VPIGAGSFLKGVIVDKNNAI
VSVGSGYAVERSIDEAIGFL
EKRLKEYDEAIKKTQGALAE
LEKRIGEVARKAQEVQQKQS
MTSFKVKK
Data type | Count |
13C chemical shifts | 753 |
15N chemical shifts | 216 |
1H chemical shifts | 606 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | PhPFD beta | 1 |
2 | PhPFD alpha | 2 |
Entity 1, PhPFD beta 117 residues - Formula weight is not available
1 | MET | GLN | ASN | ILE | PRO | PRO | GLN | VAL | GLN | ALA | ||||
2 | MET | LEU | GLY | GLN | LEU | ASP | THR | TYR | GLN | GLN | ||||
3 | GLN | LEU | GLN | LEU | VAL | ILE | GLN | GLN | LYS | GLN | ||||
4 | LYS | VAL | GLN | ALA | ASP | LEU | ASN | GLU | ALA | LYS | ||||
5 | LYS | ALA | LEU | GLU | GLU | ILE | GLU | THR | LEU | PRO | ||||
6 | ASP | ASP | ALA | GLN | ILE | TYR | LYS | THR | VAL | GLY | ||||
7 | THR | LEU | ILE | VAL | LYS | THR | THR | LYS | GLU | LYS | ||||
8 | ALA | VAL | GLN | GLU | LEU | LYS | GLU | LYS | ILE | GLU | ||||
9 | THR | LEU | GLU | VAL | ARG | LEU | ASN | ALA | LEU | ASN | ||||
10 | ARG | GLN | GLU | GLN | LYS | ILE | ASN | GLU | LYS | VAL | ||||
11 | LYS | GLU | LEU | THR | GLN | LYS | ILE | GLN | ALA | ALA | ||||
12 | LEU | ARG | PRO | PRO | THR | ALA | GLY |
Entity 2, PhPFD alpha 148 residues - Formula weight is not available
1 | MET | ALA | GLN | ASN | ASN | LYS | GLU | LEU | GLU | LYS | ||||
2 | LEU | ALA | TYR | GLU | TYR | GLN | VAL | LEU | GLN | ALA | ||||
3 | GLN | ALA | GLN | ILE | LEU | ALA | GLN | ASN | LEU | GLU | ||||
4 | LEU | LEU | ASN | LEU | ALA | LYS | ALA | GLU | VAL | GLN | ||||
5 | THR | VAL | ARG | GLU | THR | LEU | GLU | ASN | LEU | LYS | ||||
6 | LYS | ILE | GLU | GLU | GLU | LYS | PRO | GLU | ILE | LEU | ||||
7 | VAL | PRO | ILE | GLY | ALA | GLY | SER | PHE | LEU | LYS | ||||
8 | GLY | VAL | ILE | VAL | ASP | LYS | ASN | ASN | ALA | ILE | ||||
9 | VAL | SER | VAL | GLY | SER | GLY | TYR | ALA | VAL | GLU | ||||
10 | ARG | SER | ILE | ASP | GLU | ALA | ILE | GLY | PHE | LEU | ||||
11 | GLU | LYS | ARG | LEU | LYS | GLU | TYR | ASP | GLU | ALA | ||||
12 | ILE | LYS | LYS | THR | GLN | GLY | ALA | LEU | ALA | GLU | ||||
13 | LEU | GLU | LYS | ARG | ILE | GLY | GLU | VAL | ALA | ARG | ||||
14 | LYS | ALA | GLN | GLU | VAL | GLN | GLN | LYS | GLN | SER | ||||
15 | MET | THR | SER | PHE | LYS | VAL | LYS | LYS |
sample_1: PhPFD beta, [U-13C; U-15N; U-2H], 0.8 uM; PhPFD alpha, [U-2H], 0.4 uM
sample_2: PhPFD beta, [U-12C; U-15N; U-2H; 1HD-Ile;2HD-Leu;2HG-Val;HB-Ala;2HG-Thr], 0.8 uM; PhPFD alpha, [U-2H], 0.4 uM
sample_3: PhPFD beta, [U-13C; U-15N; U-2H; 1HD-Ile;2HD-Leu;2HG-Val], 0.8 uM; PhPFD alpha, [U-2H], 0.4 uM
sample_4: PhPFD beta, [U-12C; U-14N; U-2H;2HD-Leu;2HG-Val], 0.3 uM; PhPFD alpha, [U-2H], 0.15 uM
sample_5: PhPFD alpha, [U-13C; U-15N; U-2H; 1HD-Ile;1HD-Leu;1HG-Val], 0.8 uM; PhPFD beta, [U-2H], 0.4 uM
sample_6: PhPFD alpha, [U-12C; U-15N; U-2H; 1HD-Ile;2HD-Leu;2HG-Val;HB-Ala;2HG-Thr], 0.8 uM; PhPFD beta, [U-2H], 0.4 uM
sample_7: PhPFD beta, [U-2H], 0.8 uM; PhPFD alpha, [U-13C; U-15N; U-2H], 0.4 uM
sample_conditions_1: ionic strength: 0.07 M; pH: 8.5; pressure: 1 atm; temperature: 343.15 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N TROSY | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HMQC | sample_3 | isotropic | sample_conditions_1 |
2D 1H-13C HMQC | sample_4 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_4 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_5 | isotropic | sample_conditions_1 |
3D HC(C)CH-COSY | sample_5 | isotropic | sample_conditions_1 |
3D HC(CC)CH-COSY | sample_5 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_6 | isotropic | sample_conditions_1 |
3D HC(C)CH-COSY | sample_6 | isotropic | sample_conditions_1 |
3D HC(CC)CH-COSY | sample_6 | isotropic | sample_conditions_1 |
2D 1H-13C HMQC | sample_7 | isotropic | sample_conditions_1 |
2D 1H-13C HMQC | sample_7 | isotropic | sample_conditions_1 |
2D 1H-13C HMQC | sample_7 | isotropic | sample_conditions_1 |
2D 1H-13C HMQC | sample_7 | isotropic | sample_conditions_1 |
2D 1H-13C HMQC | sample_7 | isotropic | sample_conditions_1 |
ANALYSIS - chemical shift assignment
TOPSPIN - collection
NMRPipe - processing
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks