BMRB Entry 34420
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34420
MolProbity Validation Chart
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NMR-STAR v3 text file.
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Title: SH3-subunit of chicken alpha spectrin solved by NMR PubMed: 32579946
Deposition date: 2019-07-25 Original release date: 2020-08-06
Authors: Grohe, K.; Hebrank, C.; Linser, R.
Citation: Grohe, K.; Patel, S.; Hebrank, C.; Medina, S.; Klein, A.; Rovo, P.; Vasa, S.; Singh, H.; Voegeli, B.; Shaefer, L.; Linser, R.. "Protein Motional Details Revealed by Complementary Structural Biology Techniques" Structure 28, 1024-1034 (2020).
Assembly members:
entity_1, polymer, 62 residues, 7229.244 Da.
Natural source: Common Name: Pig Taxonomy ID: 9823 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Sus scrofa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21
Entity Sequences (FASTA):
entity_1: MDETGKELVLALYDYQEKSP
REVTMKKGDILTLLNSTNKD
WWKVEVNDRQGFVPAAYVKK
LD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 191 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 368 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 62 residues - 7229.244 Da.
| 1 | MET | ASP | GLU | THR | GLY | LYS | GLU | LEU | VAL | LEU | ||||
| 2 | ALA | LEU | TYR | ASP | TYR | GLN | GLU | LYS | SER | PRO | ||||
| 3 | ARG | GLU | VAL | THR | MET | LYS | LYS | GLY | ASP | ILE | ||||
| 4 | LEU | THR | LEU | LEU | ASN | SER | THR | ASN | LYS | ASP | ||||
| 5 | TRP | TRP | LYS | VAL | GLU | VAL | ASN | ASP | ARG | GLN | ||||
| 6 | GLY | PHE | VAL | PRO | ALA | ALA | TYR | VAL | LYS | LYS | ||||
| 7 | LEU | ASP |
Samples:
sample_1: SH3-domain of chicken alpha spectrin, [U-15N; U-13C], 12 mg/L
sample_conditions_1: pH: 3.5; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin v3.7, Bruker Biospin - processing
CYANA v3.98.5, Guntert, Mumenthaler and Wuthrich - structure calculation
CcpNmr Analysis v2.4.1, CCPN - chemical shift assignment
NMR spectrometers:
- Bruker Avance 3 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts