BMRB Entry 15595
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15595
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Title: A novel solution NMR structure of protein yst0336 from Saccharomyces/Northest Structural Genomics Consortium Target YT51/Ontario Center for Structural Proteomics
Deposition date: 2007-12-14 Original release date: 2008-01-15
Authors: Wu, Bin; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Gutmanas, Aleksandras; Semest, Anthony; Arrowsmith, Cheryl
Citation: Wu, Adelinda; Yee, Adelinda; Fares, Christophe; Lemak, Alexander; Gutmanas, Aleksandras; Semest, Anthony; Arrowsmith, Cheryl. "A Novel solution NMR structure of protein yst0336 from Saccharomyces cerevisiae/North Structural Genomics Consortium Target YT51/Ontario Center for Structural Proteomics Target yst0336" . ., .-..
Assembly members:
yst0336, polymer, 146 residues, Formula weight is not available
Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
yst0336: MSTFNAETADNLEDIEKQFA
VVAVEQAETYWKLLTSVPGS
KLRLTKFDDEIYENFMERFP
EYKDVERVKKFTEEELKTKE
AKERWRKFFTIFEKKIEDYN
FGTLLRTDASAEYGQFTTCF
VVRLQFYAFEIARNKHGLND
WIVGQK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 627 |
15N chemical shifts | 155 |
1H chemical shifts | 1038 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | yst0336 | 1 |
Entities:
Entity 1, yst0336 146 residues - Formula weight is not available
1 | MET | SER | THR | PHE | ASN | ALA | GLU | THR | ALA | ASP | ||||
2 | ASN | LEU | GLU | ASP | ILE | GLU | LYS | GLN | PHE | ALA | ||||
3 | VAL | VAL | ALA | VAL | GLU | GLN | ALA | GLU | THR | TYR | ||||
4 | TRP | LYS | LEU | LEU | THR | SER | VAL | PRO | GLY | SER | ||||
5 | LYS | LEU | ARG | LEU | THR | LYS | PHE | ASP | ASP | GLU | ||||
6 | ILE | TYR | GLU | ASN | PHE | MET | GLU | ARG | PHE | PRO | ||||
7 | GLU | TYR | LYS | ASP | VAL | GLU | ARG | VAL | LYS | LYS | ||||
8 | PHE | THR | GLU | GLU | GLU | LEU | LYS | THR | LYS | GLU | ||||
9 | ALA | LYS | GLU | ARG | TRP | ARG | LYS | PHE | PHE | THR | ||||
10 | ILE | PHE | GLU | LYS | LYS | ILE | GLU | ASP | TYR | ASN | ||||
11 | PHE | GLY | THR | LEU | LEU | ARG | THR | ASP | ALA | SER | ||||
12 | ALA | GLU | TYR | GLY | GLN | PHE | THR | THR | CYS | PHE | ||||
13 | VAL | VAL | ARG | LEU | GLN | PHE | TYR | ALA | PHE | GLU | ||||
14 | ILE | ALA | ARG | ASN | LYS | HIS | GLY | LEU | ASN | ASP | ||||
15 | TRP | ILE | VAL | GLY | GLN | LYS |
Samples:
sample_1: unknown function protein yst0336 from Saccharomyces cerevisiae, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 10 mM
sample_2: unknown function protein yst0336 from Saccharomyces cerevisiae, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 10 mM
sample_3: unknown function protein yst0336 from Saccharomyces cerevisiae, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; sodium azide 0.01%; benzamidine 10 mM
sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
Software:
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.95, Goddard - data analysis, peak picking
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.0, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct, Huang, Tejero, Powers and Montelione - NMR structure quality assessment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
PDB | |
DBJ | GAA26753 |
EMBL | CAA97940 CAY86735 |
GB | AAT92581 AHY77958 AJP41926 AJU23370 AJU24058 |
REF | NP_015099 |
SP | Q08971 |
TPG | DAA11211 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts