BMRB Entry 19353
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19353
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NMR-STAR v3 text file.
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Citation: Mirecka, Ewa; Shaykhalishahi, Hamed; Gauhar, Aziz; Akgul, Serife; Lecher, Justin; Willbold, Dieter; Stoldt, Matthias; Hoyer, Wolfgang. "Sequestration of a -Hairpin for Control of -Synuclein Aggregation." Angew. Chem. Int. Ed. Engl. 53, 4227-4230 (2014).
PubMed: 24623599
Assembly members:
AS69_OX, polymer, 46 residues, 5080.5829 Da.
A-Syn, polymer, 22 residues, 2200.5134 Da.
Natural source: Common Name: engineered binding protein Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: Synthetic construct
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: Champion pET302
Entity Sequences (FASTA):
AS69_OX: DGEIFYLPNLNPDQLCAFFH
SVHDDPSQSANLLAEAKKLN
DAQAPK
A-Syn: EGVLYVGSKTKEGVVHGVAT
VA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 450 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 744 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AS69 OX, 1 | 1 |
| 2 | AS69 OX, 2 | 1 |
| 3 | A-Syn | 2 |
Entities:
Entity 1, AS69 OX, 1 46 residues - 5080.5829 Da.
| 1 | ASP | GLY | GLU | ILE | PHE | TYR | LEU | PRO | ASN | LEU | ||||
| 2 | ASN | PRO | ASP | GLN | LEU | CYS | ALA | PHE | PHE | HIS | ||||
| 3 | SER | VAL | HIS | ASP | ASP | PRO | SER | GLN | SER | ALA | ||||
| 4 | ASN | LEU | LEU | ALA | GLU | ALA | LYS | LYS | LEU | ASN | ||||
| 5 | ASP | ALA | GLN | ALA | PRO | LYS |
Entity 2, A-Syn 22 residues - 2200.5134 Da.
| 1 | GLU | GLY | VAL | LEU | TYR | VAL | GLY | SER | LYS | THR | ||||
| 2 | LYS | GLU | GLY | VAL | VAL | HIS | GLY | VAL | ALA | THR | ||||
| 3 | VAL | ALA |
Samples:
AS69_CNAsyn: A-Syn, [U-13C; U-15N], 0.700 mM; AS69 0.840 mM; sodium phosphate 20 mM; NaCl 50 mM
CNAS69_Asyn: A-Syn 0.840 mM; AS69, [U-13C; U-15N], 0.700 mM; sodium phosphate 20 mM; NaCl 50 mM
Standard_30: ionic strength: 0.070 M; pH: 7.400; pressure: 1.000 atm; temperature: 303.000 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC/HMQC | AS69_CNAsyn | isotropic | Standard_30 |
| 3D HNCA | AS69_CNAsyn | isotropic | Standard_30 |
| iHNCA_CNSyn_AS69 (H[N_[CA]].onebond) | AS69_CNAsyn | isotropic | Standard_30 |
| 2D 1H-15N HSQC/HMQC | AS69_CNAsyn | isotropic | Standard_30 |
| 2D 1H-15N HSQC/HMQC | CNAS69_Asyn | isotropic | Standard_30 |
| 3D HNCA | CNAS69_Asyn | isotropic | Standard_30 |
| CNAS69_iHNCA (H[N_[CA]].onebond) | CNAS69_Asyn | isotropic | Standard_30 |
| 3D 1H-15N NOESY | CNAS69_Asyn | isotropic | Standard_30 |
| CNAS69_Syn_3DHNHA (H[N[ca[HA]]]) | CNAS69_Asyn | isotropic | Standard_30 |
| 3D 1H-13C NOESY | CNAS69_Asyn | isotropic | Standard_30 |
| 3D HCCH-COSY | CNAS69_Asyn | isotropic | Standard_30 |
| 3D HBHA(CO)NH | CNAS69_Asyn | isotropic | Standard_30 |
| CNSyn_AS69_3DHNHA (H[N[ca[HA]]]) | AS69_CNAsyn | isotropic | Standard_30 |
| 3D 1H-13C NOESY | AS69_CNAsyn | isotropic | Standard_30 |
| 3D 1H-15N NOESY | AS69_CNAsyn | isotropic | Standard_30 |
| 3D HNCO | AS69_CNAsyn | isotropic | Standard_30 |
| 2D 1H-13C HSQC/HMQC | AS69_CNAsyn | isotropic | Standard_30 |
| CNSyn_AS69_2DaromaHSQC_noesy (H[c]_H.through-space) | CNAS69_Asyn | isotropic | Standard_30 |
| 2D 1H-1H NOESY | AS69_CNAsyn | isotropic | Standard_30 |
| 2D 1H-13C HSQC/HMQC | CNAS69_Asyn | isotropic | Standard_30 |
| 3D 1H-13C NOESY | CNAS69_Asyn | isotropic | Standard_30 |
| 3D HNCO | CNAS69_Asyn | isotropic | Standard_30 |
| 2D 1H-13C HSQC/HMQC | AS69_CNAsyn | isotropic | Standard_30 |
| 2D 1H-1H NOESY | AS69_CNAsyn | isotropic | Standard_30 |
Software:
ARIA v2.3.2, Benjamin Bardiaux and Michael Nilges - assignment, structure calculation
CNS v1.21, A.T.Brunger and Micheal Nilges - structure calculation
ANALYSIS v2.2, CCPN - Assignment, Data evaluation
NMRPipe v7.9.2013.021.23.09, NIH - conversion, processing
TALOS+ v3.80F1.2012.080.14.41, Y. Shen, F. Delaglio, G. Cornilescu, and A. Bax - dihedreal angle prediction
VnmrJ v2.3A, Agilent Technologies (formerly Varian) - data recording, spectrometer operation
NMR spectrometers:
- Varian VNMRS 900 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks