BMRB Entry 18466
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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/BMR18466
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Underhaug, Jarl; Kolds, Heidi; Runager, Kasper; Nielsen, Jakob Toudahl; Srensen, Charlotte; Kristensen, Torsten; Otzen, Daniel; Karring, Henrik; Malmendal, Anders; Schitt, Birgit; Enghild, Jan; Nielsen, Niels Chr. "Mutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilization." Biochim. Biophys. Acta 1834, 2812-2822 (2013).
PubMed: 24129074
Assembly members:
Wild-type_FAS1-4, polymer, 135 residues, 14481.799 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET SUMO
Entity Sequences (FASTA):
Wild-type_FAS1-4: AGMGTVMDVLKGDNRFSMLV
AAIQSAGLTETLNREGVYTV
FAPTNEAFRALPPRERSRLL
GDAKELANILKYHIGDEILV
SGGIGALVRLKSLQGDKLEV
SLKNNVVSVNKEPVAEPDIM
ATNGVVHVITNVLQP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 498 |
| 15N chemical shifts | 129 |
| 1H chemical shifts | 860 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Wild-type FAS1-4 | 1 |
Entities:
Entity 1, Wild-type FAS1-4 135 residues - 14481.799 Da.
| 1 | ALA | GLY | MET | GLY | THR | VAL | MET | ASP | VAL | LEU | ||||
| 2 | LYS | GLY | ASP | ASN | ARG | PHE | SER | MET | LEU | VAL | ||||
| 3 | ALA | ALA | ILE | GLN | SER | ALA | GLY | LEU | THR | GLU | ||||
| 4 | THR | LEU | ASN | ARG | GLU | GLY | VAL | TYR | THR | VAL | ||||
| 5 | PHE | ALA | PRO | THR | ASN | GLU | ALA | PHE | ARG | ALA | ||||
| 6 | LEU | PRO | PRO | ARG | GLU | ARG | SER | ARG | LEU | LEU | ||||
| 7 | GLY | ASP | ALA | LYS | GLU | LEU | ALA | ASN | ILE | LEU | ||||
| 8 | LYS | TYR | HIS | ILE | GLY | ASP | GLU | ILE | LEU | VAL | ||||
| 9 | SER | GLY | GLY | ILE | GLY | ALA | LEU | VAL | ARG | LEU | ||||
| 10 | LYS | SER | LEU | GLN | GLY | ASP | LYS | LEU | GLU | VAL | ||||
| 11 | SER | LEU | LYS | ASN | ASN | VAL | VAL | SER | VAL | ASN | ||||
| 12 | LYS | GLU | PRO | VAL | ALA | GLU | PRO | ASP | ILE | MET | ||||
| 13 | ALA | THR | ASN | GLY | VAL | VAL | HIS | VAL | ILE | THR | ||||
| 14 | ASN | VAL | LEU | GLN | PRO |
Samples:
sample_1: Wild-type_FAS1-4, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; DSS 0.5 mM; sodium azide 0.5%; arginine 50 mM; glutamate 50 mM; H2O 90%; D2O 10%
sample_2: Wild-type_FAS1-4, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; DSS 0.5 mM; sodium azide 0.5%; arginine 50 mM; glutamate 50 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 300 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-TOCSY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D IPAP-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D IPAP-HSQC | sample_2 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - peak picking
TALOS, Cornilescu, Delaglio and Bax - data analysis
REDCAT, Valafar, Homayoun, and James H. Prestegard - data analysis
ARIA, Linge, O'Donoghue and Nilges - structure solution
CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks