BMRB Entry 30877
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30877
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Magic Angle Spinning NMR Structure of Human Cofilin-2 Assembled on Actin Filaments PubMed: 35440100
Deposition date: 2021-03-10 Original release date: 2022-04-15
Authors: Kraus, J.; Polenova, T.; Perilla, J.; Xu, C.
Citation: Kraus, Jodi; Russell, Ryan; Kudryashova, Elena; Xu, Chaoyi; Katyal, Nidhi; Perilla, Juan; Kudryashov, Dmitri; Polenova, Tatyana. "Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode" Nat. Commun. 13, 2114-2114 (2022).
Assembly members:
entity_1, polymer, 166 residues, 18765.627 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_1: MASGVTVNDEVIKVFNDMKV
RKSSTQEEIKKRKKAVLFCL
SDDKRQIIVEEAKQILVGDI
GDTVEDPYTSFVKLLPLNDC
RYALYDATYETKESKKEDLV
FIFWAPESAPLKSKMIYASS
KDAIKKKFTGIKHEWQVNGL
DDIKDRSTLGEKLGGNVVVS
LEGKPL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 779 |
| 15N chemical shifts | 163 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 166 residues - 18765.627 Da.
| 1 | MET | ALA | SER | GLY | VAL | THR | VAL | ASN | ASP | GLU | ||||
| 2 | VAL | ILE | LYS | VAL | PHE | ASN | ASP | MET | LYS | VAL | ||||
| 3 | ARG | LYS | SER | SER | THR | GLN | GLU | GLU | ILE | LYS | ||||
| 4 | LYS | ARG | LYS | LYS | ALA | VAL | LEU | PHE | CYS | LEU | ||||
| 5 | SER | ASP | ASP | LYS | ARG | GLN | ILE | ILE | VAL | GLU | ||||
| 6 | GLU | ALA | LYS | GLN | ILE | LEU | VAL | GLY | ASP | ILE | ||||
| 7 | GLY | ASP | THR | VAL | GLU | ASP | PRO | TYR | THR | SER | ||||
| 8 | PHE | VAL | LYS | LEU | LEU | PRO | LEU | ASN | ASP | CYS | ||||
| 9 | ARG | TYR | ALA | LEU | TYR | ASP | ALA | THR | TYR | GLU | ||||
| 10 | THR | LYS | GLU | SER | LYS | LYS | GLU | ASP | LEU | VAL | ||||
| 11 | PHE | ILE | PHE | TRP | ALA | PRO | GLU | SER | ALA | PRO | ||||
| 12 | LEU | LYS | SER | LYS | MET | ILE | TYR | ALA | SER | SER | ||||
| 13 | LYS | ASP | ALA | ILE | LYS | LYS | LYS | PHE | THR | GLY | ||||
| 14 | ILE | LYS | HIS | GLU | TRP | GLN | VAL | ASN | GLY | LEU | ||||
| 15 | ASP | ASP | ILE | LYS | ASP | ARG | SER | THR | LEU | GLY | ||||
| 16 | GLU | LYS | LEU | GLY | GLY | ASN | VAL | VAL | VAL | SER | ||||
| 17 | LEU | GLU | GLY | LYS | PRO | LEU |
Samples:
sample_1: human cofilin-2, [U-13C; U-15N], 20.8 % w/w; F-actin, NA-actin, 79.2 % w/w
sample_2: human cofilin-2, [1,6-13C]-glucose, U-15N, 20.8 % w/w; F-actin, NA-actin, 79.2 % w/w
sample_3: human cofilin-2, [2-13C]-glucose, U-15N, 20.8 % w/w; F-actin, NA-actin, 79.2 % w/w
sample_conditions_1: ionic strength: 50 mM; pH: 6.6; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| Exp1_CORD50ms | sample_1 | isotropic | sample_conditions_1 |
| Exp2_CORD200ms | sample_1 | isotropic | sample_conditions_1 |
| Exp3_CORD50ms | sample_2 | isotropic | sample_conditions_1 |
| Exp4_CORD200ms | sample_2 | isotropic | sample_conditions_1 |
| Exp5_CORD500ms | sample_2 | isotropic | sample_conditions_1 |
| Exp6_CORD50ms | sample_3 | isotropic | sample_conditions_1 |
| Exp7_CORD200ms | sample_3 | isotropic | sample_conditions_1 |
| Exp8_CORD500ms | sample_3 | isotropic | sample_conditions_1 |
| Exp9_PAINCP | sample_3 | isotropic | sample_conditions_1 |
| Exp10_NCACX2d | sample_1 | isotropic | sample_conditions_1 |
| Exp11_NCACX3d | sample_1 | isotropic | sample_conditions_1 |
| Exp12_NCOCX2d | sample_1 | isotropic | sample_conditions_1 |
| Exp13_NCOCX3d | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Rowland NMR Toolkit (RNMRTK), Hoch and Stern - processing
CcpNmr Analysis, CCPN - chemical shift assignment, peak picking
TALOS-N, Cornilescu, Delaglio and Bax - structure calculation
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMR spectrometers:
- Bruker AVANCE III 850 MHz