BMRB Entry 25987
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25987
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Title: Solution structure of the T119M variant of transthyretin in its monomeric state PubMed: 27885756
Deposition date: 2016-03-09 Original release date: 2017-05-08
Authors: Kim, Jin Hae; Oroz, Javier; Zweckstetter, Markus
Citation: Kim, Jin Hae; Oroz, Javier; Zweckstetter, Markus. "Structure of Monomeric Transthyretin Carrying the Clinically Important T119M Mutation." Angew. Chem. Int. Ed. Engl. 55, 16168-16171 (2016).
Assembly members:
T119M_M-TTR, polymer, 127 residues, 13809.627 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):
T119M_M-TTR: GPTGTGESKCPLMVKVLDAV
RGSPAINVAVHVFRKAADDT
WEPFASGKTSESGELHGLTT
EEEFVEGIYKVEIDTKSYWK
ALGISPMHEHAEVVFTANDS
GPRRYTIAAMLSPYSYSTMA
VVTNPKE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 381 |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 798 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 127 residues - 13809.627 Da.
| 1 | GLY | PRO | THR | GLY | THR | GLY | GLU | SER | LYS | CYS | ||||
| 2 | PRO | LEU | MET | VAL | LYS | VAL | LEU | ASP | ALA | VAL | ||||
| 3 | ARG | GLY | SER | PRO | ALA | ILE | ASN | VAL | ALA | VAL | ||||
| 4 | HIS | VAL | PHE | ARG | LYS | ALA | ALA | ASP | ASP | THR | ||||
| 5 | TRP | GLU | PRO | PHE | ALA | SER | GLY | LYS | THR | SER | ||||
| 6 | GLU | SER | GLY | GLU | LEU | HIS | GLY | LEU | THR | THR | ||||
| 7 | GLU | GLU | GLU | PHE | VAL | GLU | GLY | ILE | TYR | LYS | ||||
| 8 | VAL | GLU | ILE | ASP | THR | LYS | SER | TYR | TRP | LYS | ||||
| 9 | ALA | LEU | GLY | ILE | SER | PRO | MET | HIS | GLU | HIS | ||||
| 10 | ALA | GLU | VAL | VAL | PHE | THR | ALA | ASN | ASP | SER | ||||
| 11 | GLY | PRO | ARG | ARG | TYR | THR | ILE | ALA | ALA | MET | ||||
| 12 | LEU | SER | PRO | TYR | SER | TYR | SER | THR | MET | ALA | ||||
| 13 | VAL | VAL | THR | ASN | PRO | LYS | GLU |
Samples:
sample_1: T119M M-TTR, [U-13C; U-15N], 0.6 – 1.2 mM; MES 50 mM; sodium chloride 100 mM; DTT 5 mM; DSS 0.1 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Oxford Avance 700 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts