BMRB Entry 15777
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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/BMR15777
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Title: Solution Structure of IG-Like Domain 23 from Human Filamin A PubMed: 19293932
Deposition date: 2008-05-16 Original release date: 2009-05-22
Authors: Heikkinen, Outi; Kupiainen, Olga; Ylanne, Jari; Kilpelainen, Ilkka
Citation: Nakamura, Fumihiko; Heikkinen, Outi; Pentikainen, Olli; Osborn, Teresia; Kasza, Karen; Weitz, David; Kupiainen, Olga; Permi, Perttu; Kilpelainen, Ilkka; Ylanne, Jari; Hartwig, John; Stossel, Thomas. "Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations" PLoS ONE 4, 4928-4928 (2009).
Assembly members:
FLNA23, polymer, 99 residues, 9989.371 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):
FLNA23: GAMGDPGLVSAYGAGLEGGV
TGNPAEFVVNTSNAGAGALS
VTIDGPSKVKMDCQECPEGY
RVTYTPMAPGSYLISIKYGG
PYHIGGSPFKAKVTGPRLV
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 374 |
15N chemical shifts | 92 |
1H chemical shifts | 627 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | FLNA23 | 1 |
Entities:
Entity 1, FLNA23 99 residues - 9989.371 Da.
1 | GLY | ALA | MET | GLY | ASP | PRO | GLY | LEU | VAL | SER | ||||
2 | ALA | TYR | GLY | ALA | GLY | LEU | GLU | GLY | GLY | VAL | ||||
3 | THR | GLY | ASN | PRO | ALA | GLU | PHE | VAL | VAL | ASN | ||||
4 | THR | SER | ASN | ALA | GLY | ALA | GLY | ALA | LEU | SER | ||||
5 | VAL | THR | ILE | ASP | GLY | PRO | SER | LYS | VAL | LYS | ||||
6 | MET | ASP | CYS | GLN | GLU | CYS | PRO | GLU | GLY | TYR | ||||
7 | ARG | VAL | THR | TYR | THR | PRO | MET | ALA | PRO | GLY | ||||
8 | SER | TYR | LEU | ILE | SER | ILE | LYS | TYR | GLY | GLY | ||||
9 | PRO | TYR | HIS | ILE | GLY | GLY | SER | PRO | PHE | LYS | ||||
10 | ALA | LYS | VAL | THR | GLY | PRO | ARG | LEU | VAL |
Samples:
sample_1: FLNA23, [U-13C; U-15N], 1 ± 0.2 mM; Sodium phosphate 20 mM; Sodium chloride 150 mM; DTT 1 mM; Sodium azide 2 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
iHNCA | sample_1 | isotropic | sample_conditions_1 |
iHNCACB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMR v6.1C, Varian - collection, data analysis, processing
SPARKY v3.110, Goddard - chemical shift assignment, data analysis, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER v8.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Related Database Links:
PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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or all simulated shifts