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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/BMR25411
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Kroupa, Tomas; Dolezal, Michal; Prchal, Jan; Ruml, Tomas; Hrabal, Richard. "Mason-Pfizer monkey virus matrix protein mutants - structural view of impaired membrane interaction" J. Mol. Biol. ., .-..
Assembly members:
MPMV_MA_T41I_T78I, polymer, 125 residues, 14737.889 Da.
Natural source: Common Name: Simian retrovirus Taxonomy ID: 11855 Superkingdom: Viruses Kingdom: not available Genus/species: Betaretrovirus Mason-Pfizer monkey virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-22b
Entity Sequences (FASTA):
MPMV_MA_T41I_T78I: XGQELSQHERYVEQLKQALK
TRGVKVKYADLLKFFDFVKD
ICPWFPQEGTIDIKRWRRVG
DCFQDYYNTFGPEKVPVIAF
SYWNLIKELIDKKEVNPQVM
AAVAQTEEILKSNSQTDLEH
HHHHH
Data type | Count |
13C chemical shifts | 374 |
15N chemical shifts | 100 |
1H chemical shifts | 687 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MPMV MA T41I T78I | 1 |
Entity 1, MPMV MA T41I T78I 125 residues - 14737.889 Da.
1 | MYR | GLY | GLN | GLU | LEU | SER | GLN | HIS | GLU | ARG | ||||
2 | TYR | VAL | GLU | GLN | LEU | LYS | GLN | ALA | LEU | LYS | ||||
3 | THR | ARG | GLY | VAL | LYS | VAL | LYS | TYR | ALA | ASP | ||||
4 | LEU | LEU | LYS | PHE | PHE | ASP | PHE | VAL | LYS | ASP | ||||
5 | ILE | CYS | PRO | TRP | PHE | PRO | GLN | GLU | GLY | THR | ||||
6 | ILE | ASP | ILE | LYS | ARG | TRP | ARG | ARG | VAL | GLY | ||||
7 | ASP | CYS | PHE | GLN | ASP | TYR | TYR | ASN | THR | PHE | ||||
8 | GLY | PRO | GLU | LYS | VAL | PRO | VAL | ILE | ALA | PHE | ||||
9 | SER | TYR | TRP | ASN | LEU | ILE | LYS | GLU | LEU | ILE | ||||
10 | ASP | LYS | LYS | GLU | VAL | ASN | PRO | GLN | VAL | MET | ||||
11 | ALA | ALA | VAL | ALA | GLN | THR | GLU | GLU | ILE | LEU | ||||
12 | LYS | SER | ASN | SER | GLN | THR | ASP | LEU | GLU | HIS | ||||
13 | HIS | HIS | HIS | HIS | HIS |
sample_1: MPMV_MA_T41I_T78I, [U-99% 13C; U-99% 15N, NA-MYR], 0.4 0.7 mM; sodium chloride 300 mM; sodium phosphate 100 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 1 M; pH: 6; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
CcpNmr_Analysis v2.3, CCPN - chemical shift assignment
TOPSPIN v3.2, Bruker Biospin - collection, processing
X-PLOR_NIH, Brunger - structure solution
Download HSQC peak lists in one of the following formats:
CSV: Backbone
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