BMRB Entry 16659
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16659
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Title: Assignment and structural characterization of intrinsically disordered CDK inhibitor phosphoSic1 from yeast PubMed: 20399186
Deposition date: 2009-12-30 Original release date: 2010-05-05
Authors: Mittag, Tanja; Choy, Wing-Yiu; Marsh, Joseph; Orlicky, Stephen; Grishaev, Alexander; Lin, Hong; Sicheri, Frank; Tyers, Mike; Forman-Kay, Julie
Citation: Mittag, Tanja; Marsh, Joseph; Grishaev, Alexander; Orlicky, Stephen; Lin, Hong; Sicheri, Frank; Tyers, Mike; Forman-Kay, Julie. "Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase." Structure (Cambridge, MA, U. S.) 18, 494-506 (2010).
Assembly members:
pSic1, polymer, 92 residues, 10195 Da.
pSic1_G-1X, polymer, 92 residues, Formula weight is not available
pSic1_N21X, polymer, 92 residues, Formula weight is not available
pSic1_S38X, polymer, 92 residues, Formula weight is not available
pSic1_N64X, polymer, 92 residues, Formula weight is not available
pSic1_P83X, polymer, 92 residues, Formula weight is not available
pSic1_T90X, polymer, 92 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 Vector: pGEX
Entity Sequences (FASTA):
pSic1: GSMTPSXPPRSRGTRYLAQP
SGNTSSSALMQGQKXPQKPS
QNLVPVXPSTTKSFKNAPLL
APPNSNMGMTXPFNGLTXPQ
RXPFPKSSVKRT
pSic1_G-1X: XSMTPSXPPRSRGTRYLAQP
SGNTSSSALMQGQKXPQKPS
QNLVPVXPSTTKSFKNAPLL
APPNSNMGMTXPFNGLTXPQ
RXPFPKSSVKRT
pSic1_N21X: GSMTPSXPPRSRGTRYLAQP
SGXTSSSALMQGQKXPQKPS
QNLVPVXPSTTKSFKNAPLL
APPNSNMGMTXPFNGLTXPQ
RXPFPKSSVKRT
pSic1_S38X: GSMTPSXPPRSRGTRYLAQP
SGNTSSSALMQGQKXPQKPX
QNLVPVXPSTTKSFKNAPLL
APPNSNMGMTXPFNGLTXPQ
RXPFPKSSVKRT
pSic1_N64X: GSMTPSXPPRSRGTRYLAQP
SGNTSSSALMQGQKXPQKPS
QNLVPVXPSTTKSFKNAPLL
APPNSXMGMTXPFNGLTXPQ
RXPFPKSSVKRT
pSic1_P83X: GSMTPSXPPRSRGTRYLAQP
SGNTSSSALMQGQKXPQKPS
QNLVPVXPSTTKSFKNAPLL
APPNSNMGMTXPFNGLTXPQ
RXPFXKSSVKRT
pSic1_T90X: GSMTPSXPPRSRGTRYLAQP
SGNTSSSALMQGQKXPQKPS
QNLVPVXPSTTKSFKNAPLL
APPNSNMGMTXPFNGLTXPQ
RXPFPKSSVKRX
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 171 |
15N chemical shifts | 75 |
1H chemical shifts | 75 |
heteronuclear NOE values | 74 |
residual dipolar couplings | 63 |
T1 relaxation values | 74 |
T2 relaxation values | 74 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | pSic1 | 1 |
Entities:
Entity 1, pSic1 92 residues - 10195 Da.
The first two residues represent a non-native artifact from cleavage of an affinity tag and are therefore numbered -1 and 0. Residue M1 is the actual beginning of the native Sic1 sequence. The construct used represents the first 90 residues of Sic1, the so-called targeting region. Residues 5, 33 and 45 are phosphoThr, 69,76 and 80 phosphoSer.
1 | GLY | SER | MET | THR | PRO | SER | TPO | PRO | PRO | ARG | ||||
2 | SER | ARG | GLY | THR | ARG | TYR | LEU | ALA | GLN | PRO | ||||
3 | SER | GLY | ASN | THR | SER | SER | SER | ALA | LEU | MET | ||||
4 | GLN | GLY | GLN | LYS | TPO | PRO | GLN | LYS | PRO | SER | ||||
5 | GLN | ASN | LEU | VAL | PRO | VAL | TPO | PRO | SER | THR | ||||
6 | THR | LYS | SER | PHE | LYS | ASN | ALA | PRO | LEU | LEU | ||||
7 | ALA | PRO | PRO | ASN | SER | ASN | MET | GLY | MET | THR | ||||
8 | SEP | PRO | PHE | ASN | GLY | LEU | THR | SEP | PRO | GLN | ||||
9 | ARG | SEP | PRO | PHE | PRO | LYS | SER | SER | VAL | LYS | ||||
10 | ARG | THR |
Samples:
sample_1: pSic1, [U-13C; U-15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.02%; EDTA 1 mM; DSS 1 mM; H2O 90%; D2O 10%
sample_2: pSic1, [U-15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.02%; EDTA 1 mM; DSS 1 mM; H2O 90%; D2O 10%
sample_3: pSic1, [U-15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.02%; EDTA 1 mM; DSS 1 mM; PEG(C12E5)/hexanol 0.08 v/v; H2O 90%; D2O 10%
sample_4: pSic1_G-1X, [U-15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.02%; EDTA 1 mM; DSS 1 mM; H2O 90%; D2O 10%
sample_5: pSic1_N21X, [U-15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.02%; EDTA 1 mM; DSS 1 mM; H2O 90%; D2O 10%
sample_6: pSic1_S38X, [U-15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.02%; EDTA 1 mM; DSS 1 mM; H2O 90%; D2O 10%
sample_7: pSic1_N64X, [U-15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.02%; EDTA 1 mM; DSS 1 mM; H2O 90%; D2O 10%
sample_8: pSic1_P83X, [U-15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.02%; EDTA 1 mM; DSS 1 mM; H2O 90%; D2O 10%
sample_9: pSic1_T90X, [U-15N], 0.5 mM; potassium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.02%; EDTA 1 mM; DSS 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.2 M; pH: 7.0; pressure: 1 atm; temperature: 278 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
pseudo3D 15N T1 | sample_2 | isotropic | sample_conditions_1 |
pseudo3D 15N T1rho | sample_2 | isotropic | sample_conditions_1 |
pseudo3D 1H-15N hetNOE | sample_2 | isotropic | sample_conditions_1 |
2D 1H-15N IPAP | sample_3 | anisotropic | sample_conditions_1 |
pseudo3D NH R2 for PRE | sample_4 | isotropic | sample_conditions_1 |
pseudo3D NH R2 for PRE | sample_5 | isotropic | sample_conditions_1 |
pseudo3D NH R2 for PRE | sample_6 | isotropic | sample_conditions_1 |
pseudo3D NH R2 for PRE | sample_7 | isotropic | sample_conditions_1 |
pseudo3D NH R2 for PRE | sample_8 | isotropic | sample_conditions_1 |
pseudo3D NH R2 for PRE | sample_9 | isotropic | sample_conditions_1 |
Software:
ENSEMBLE, Marsh, Choy, Forman-Kay - ensemble generation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment
FuDA, Kristensen and Hansen - peak integration, RDC analysis
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts