BMRB Entry 30880
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30880
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Title: NMR structure of the Human T-cell leukemia virus 1 matrix protein PubMed: 34298060
Deposition date: 2021-03-15 Original release date: 2021-09-17
Authors: Herrmann, D.; Saad, J.
Citation: Herrmann, Dominik; Zhou, Lynne; Hanson, Heather; Willkomm, Nora; Mansky, Louis; Saad, Jamil. "Structural Insights into the Mechanism of Human T-cell Leukemia Virus Type 1 Gag Targeting to the Plasma Membrane for Assembly" J. Mol. Biol. 433, 167161-167161 (2021).
Assembly members:
entity_1, polymer, 105 residues, 12026.986 Da.
Natural source: Common Name: HTLV-1 Taxonomy ID: 11908 Superkingdom: Viruses Kingdom: not available Genus/species: Deltaretrovirus HTLV-1
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MGRIFSRSASPIPRPPRGLA
AHHWLNFLQAAYRLEPGPSS
YDFHQLKKFLKIALETPVWI
CPINYSLLASLLPKGYPGRV
NEILHILIQTQAQIPSRPAH
HHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 439 |
| 15N chemical shifts | 95 |
| 1H chemical shifts | 698 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 105 residues - 12026.986 Da.
| 1 | MET | GLY | ARG | ILE | PHE | SER | ARG | SER | ALA | SER | ||||
| 2 | PRO | ILE | PRO | ARG | PRO | PRO | ARG | GLY | LEU | ALA | ||||
| 3 | ALA | HIS | HIS | TRP | LEU | ASN | PHE | LEU | GLN | ALA | ||||
| 4 | ALA | TYR | ARG | LEU | GLU | PRO | GLY | PRO | SER | SER | ||||
| 5 | TYR | ASP | PHE | HIS | GLN | LEU | LYS | LYS | PHE | LEU | ||||
| 6 | LYS | ILE | ALA | LEU | GLU | THR | PRO | VAL | TRP | ILE | ||||
| 7 | CYS | PRO | ILE | ASN | TYR | SER | LEU | LEU | ALA | SER | ||||
| 8 | LEU | LEU | PRO | LYS | GLY | TYR | PRO | GLY | ARG | VAL | ||||
| 9 | ASN | GLU | ILE | LEU | HIS | ILE | LEU | ILE | GLN | THR | ||||
| 10 | GLN | ALA | GLN | ILE | PRO | SER | ARG | PRO | ALA | HIS | ||||
| 11 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: sodium chloride 100 mM; sodium phosphate 50 mM; TCEP 2 mM; HTLV-1 Matrix, [U-99% 13C; U-99% 15N], 400 uM
sample_2: sodium chloride 100 mM; sodium phosphate 50 mM; TCEP 2 mM; HTLV-1 Matrix, [U-99% 13C; U-99% 15N], 320 uM
sample_3: sodium chloride 100 mM; sodium phosphate 50 mM; TCEP 2 mM; HTLV-1 Matrix, [U-99% 15N], 500 uM
sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-separated NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 13C-separated NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY arom. | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY ali. | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-separated TOCSY | sample_3 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert P. - refinement
CcpNmr Analysis v2.4, CCPN - chemical shift assignment
CARA v1.9.1.2, Keller and Wuthrich - processing
UNIO v10, Torsten Herrmann - chemical shift assignment
TopSpin, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker AVANCE II 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts