BMRB Entry 26520
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26520
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Title: Studying Invisible Excited Protein States in Slow Exchange with a Major State Conformation PubMed: 22554188
Deposition date: 2015-02-24 Original release date: 2015-03-09
Authors: Vallurupalli, Pramodh; Bouvignies, Guillaume; Kay, Lewis
Citation: Vallurupalli, Pramodh; Bouvignies, Guillaume; Kay, Lewis. "Studying Invisible Excited Protein States in Slow Exchange with a Major State Conformation" J. Am. Chem. Soc. 134, 8148-8161 (2012).
Assembly members:
A39G_FF, polymer, 71 residues, Formula weight is not available
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 Vector: pRSET
Entity Sequences (FASTA):
A39G_FF: ESQPAKKTYTWNTKEEAKQA
FKELLKEKRVPSNASWEQAM
KMIINDPRYSALAKLSEKKQ
AFNAYKVQTEK
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| T1 relaxation values | 65 |
| T2 relaxation values | 130 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | A39G FF domain | 1 |
Entities:
Entity 1, A39G FF domain 71 residues - Formula weight is not available
| 1 | GLU | SER | GLN | PRO | ALA | LYS | LYS | THR | TYR | THR | ||||
| 2 | TRP | ASN | THR | LYS | GLU | GLU | ALA | LYS | GLN | ALA | ||||
| 3 | PHE | LYS | GLU | LEU | LEU | LYS | GLU | LYS | ARG | VAL | ||||
| 4 | PRO | SER | ASN | ALA | SER | TRP | GLU | GLN | ALA | MET | ||||
| 5 | LYS | MET | ILE | ILE | ASN | ASP | PRO | ARG | TYR | SER | ||||
| 6 | ALA | LEU | ALA | LYS | LEU | SER | GLU | LYS | LYS | GLN | ||||
| 7 | ALA | PHE | ASN | ALA | TYR | LYS | VAL | GLN | THR | GLU | ||||
| 8 | LYS |
Samples:
sample_1: A39G_FF, [U-100% 15N], 2 mM; sodium acetate 50 mM; NaCl 100 mM; H2O 90%; D2O 10%
sample_conditions_1: temperature: 274 K; pH: 5.7; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HMQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - Visualization
CATIA, Bloch McConnell - data analysis
NMRpipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian Inova 500 MHz