BMRB Entry 19596
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19596
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Title: C-terminal disordered region of the pancreatic duodenal homeobox protein 1 PubMed: 24333248
Deposition date: 2013-11-01 Original release date: 2014-02-11
Authors: Sahu, Debashish; Bastidas, Monique; Showalter, Scott
Citation: Sahu, Debashish; Bastidas, Monique; Showalter, Scott. "Generating NMR chemical shift assignments of intrinsically disordered proteins using carbon-detected NMR methods." Anal. Biochem. 449C, 17-25 (2013).
Assembly members:
pdx1c, polymer, 83 residues, 8088.9849 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):
pdx1c: GPGEEDKKRGGGTAVGGGGV
AEPEQDCAVTSGEELLALPP
PPPPGGAVPPAAPVAAREGR
LPPGLSASPQPSSVAPRRPQ
EPR
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 261 |
15N chemical shifts | 74 |
1H chemical shifts | 342 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | c-terminal of pancreatic duodenal homeobox protein 1 | 1 |
Entities:
Entity 1, c-terminal of pancreatic duodenal homeobox protein 1 83 residues - 8088.9849 Da.
1 | GLY | PRO | GLY | GLU | GLU | ASP | LYS | LYS | ARG | GLY | ||||
2 | GLY | GLY | THR | ALA | VAL | GLY | GLY | GLY | GLY | VAL | ||||
3 | ALA | GLU | PRO | GLU | GLN | ASP | CYS | ALA | VAL | THR | ||||
4 | SER | GLY | GLU | GLU | LEU | LEU | ALA | LEU | PRO | PRO | ||||
5 | PRO | PRO | PRO | PRO | GLY | GLY | ALA | VAL | PRO | PRO | ||||
6 | ALA | ALA | PRO | VAL | ALA | ALA | ARG | GLU | GLY | ARG | ||||
7 | LEU | PRO | PRO | GLY | LEU | SER | ALA | SER | PRO | GLN | ||||
8 | PRO | SER | SER | VAL | ALA | PRO | ARG | ARG | PRO | GLN | ||||
9 | GLU | PRO | ARG |
Samples:
sample_1: pdx1c, [U-99% 13C; U-99% 15N], 0.8 ± 0.2 mM; cacodylate buffer pH 6.5 50 mM; potassium chloride 50 mM; DTT 1 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D (HN-flip)N(CA)CON | sample_1 | isotropic | sample_conditions_1 |
3D (HN-flip)N(CA)NCO | sample_1 | isotropic | sample_conditions_1 |
2D (HN-flip)CON | sample_1 | isotropic | sample_conditions_1 |
2D (HACA)CON | sample_1 | isotropic | sample_conditions_1 |
2D CACON THR | sample_1 | isotropic | sample_conditions_1 |
2D CANCO THR | sample_1 | isotropic | sample_conditions_1 |
2D CACON TAVI | sample_1 | isotropic | sample_conditions_1 |
2D CANCO TAVI | sample_1 | isotropic | sample_conditions_1 |
2D CACON SER | sample_1 | isotropic | sample_conditions_1 |
2D CANCO SER | sample_1 | isotropic | sample_conditions_1 |
2D CACON LEU/ALA | sample_1 | isotropic | sample_conditions_1 |
2D CANCO LEU/ALA | sample_1 | isotropic | sample_conditions_1 |
2D CACON ALA | sample_1 | isotropic | sample_conditions_1 |
2D CANCO ALA | sample_1 | isotropic | sample_conditions_1 |
2D CACON GLY | sample_1 | isotropic | sample_conditions_1 |
2D CANCO GLY | sample_1 | isotropic | sample_conditions_1 |
2D CACON GLU | sample_1 | isotropic | sample_conditions_1 |
2D CANCO GLU | sample_1 | isotropic | sample_conditions_1 |
2D CANCO ASP | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
SPARKY v3.113, Goddard - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
DBJ | BAG74161 |
EMBL | CAA68169 |
GB | AAA74012 AAA88820 AAB47101 AAB88463 AAC05157 |
REF | NP_000200 NP_001074947 XP_001096758 XP_002748960 XP_002824168 |
SP | A1YF08 A1YG85 A2T756 P52945 |