BMRB Entry 26011
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26011
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Title: Apo solution structure of Hop TPR2A
Deposition date: 2016-03-23 Original release date: 2017-03-23
Authors: Darby, John; Vidler, Lewis; Simpson, Peter; Matthews, Steven; Sharp, Swee; Pearl, Laurence; Hoelder, Swen; Workman, Paul
Citation: Darby, John; Vidler, Lewis; Simpson, Peter; Matthews, Steven; Sharp, Swee; Pearl, Laurence; Hoelder, Swen; Workman, Paul. "Solution structure of the Hop TPR 2A domain and validation of novel approaches to inhibitor indentification by NMR, biochemical and in silico screening" Not known ., .-..
Assembly members:
entity, polymer, 139 residues, 15569.708 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):
entity: GPHMASLPENKKQALKEKEL
GNDAYKKKDFDTALKHYDKA
KELDPTNMTYITNQAAVYFE
KGDYNKCRELCEKAIEVGRE
NREDYRQIAKAYARIGNSYF
KEEKYKDAIHFYNKSLAEHR
TPDVLKKCQQAEKILKEQE
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 607 |
| 15N chemical shifts | 131 |
| 1H chemical shifts | 934 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 139 residues - 15569.708 Da.
| 1 | GLY | PRO | HIS | MET | ALA | SER | LEU | PRO | GLU | ASN | ||||
| 2 | LYS | LYS | GLN | ALA | LEU | LYS | GLU | LYS | GLU | LEU | ||||
| 3 | GLY | ASN | ASP | ALA | TYR | LYS | LYS | LYS | ASP | PHE | ||||
| 4 | ASP | THR | ALA | LEU | LYS | HIS | TYR | ASP | LYS | ALA | ||||
| 5 | LYS | GLU | LEU | ASP | PRO | THR | ASN | MET | THR | TYR | ||||
| 6 | ILE | THR | ASN | GLN | ALA | ALA | VAL | TYR | PHE | GLU | ||||
| 7 | LYS | GLY | ASP | TYR | ASN | LYS | CYS | ARG | GLU | LEU | ||||
| 8 | CYS | GLU | LYS | ALA | ILE | GLU | VAL | GLY | ARG | GLU | ||||
| 9 | ASN | ARG | GLU | ASP | TYR | ARG | GLN | ILE | ALA | LYS | ||||
| 10 | ALA | TYR | ALA | ARG | ILE | GLY | ASN | SER | TYR | PHE | ||||
| 11 | LYS | GLU | GLU | LYS | TYR | LYS | ASP | ALA | ILE | HIS | ||||
| 12 | PHE | TYR | ASN | LYS | SER | LEU | ALA | GLU | HIS | ARG | ||||
| 13 | THR | PRO | ASP | VAL | LEU | LYS | LYS | CYS | GLN | GLN | ||||
| 14 | ALA | GLU | LYS | ILE | LEU | LYS | GLU | GLN | GLU |
Samples:
sample_1: entity, [U-13C; U-15N], 1.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%
sample_2: entity, [U-13C; U-15N], 1.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 0.01%
sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCCO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)C(CCO)NH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCD)H-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.1, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis
TALOS, Cornilescu, Delaglio and Bax - data analysis
ARIA, Linge, O'Donoghue and Nilges - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts