BMRB Entry 15924
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15924
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Title: Filamin A Ig-like domains 16-17 PubMed: 19636946
Deposition date: 2008-08-19 Original release date: 2009-01-15
Authors: Heikkinen, Outi; Kilpelainen, Ilkka; Koskela, Harri; Permi, Perttu; Heikkinen, Sami; Ylanne, Jari
Citation: Heikkinen, Outi; Permi, Perttu; Koskela, Harri; Ylanne, Jari; Kilpelainen, Ilkka. "1H, 13C and 15N resonance assignments of the human filamin A tandem immunoglobulin-like domains 16-17 and 18-19" Biomol. NMR Assignments 3, 53-56 (2009).
Assembly members:
FLNa16-17, polymer, 188 residues, 19994.4375 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):
FLNa16-17: GAMAPERPLVGVNGLDVTSL
RPFDLVIPFTIKKGEITGEV
RMPSGKVAQPTITDNKDGTV
TVRYAPSEAGLHEMDIRYDN
MHIPGSPLQFYVDYVNCGHV
TAYGPGLTHGVVNKPATFTV
NTKDAGEGGLSLAIEGPSKA
EISCTDNQDGTCSVSYLPVL
PGDYSILVKYNEQHVPGSPF
TARVTGDD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 590 |
| 15N chemical shifts | 183 |
| 1H chemical shifts | 1261 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FLNa16-17 | 1 |
Entities:
Entity 1, FLNa16-17 188 residues - 19994.4375 Da.
| 1 | GLY | ALA | MET | ALA | PRO | GLU | ARG | PRO | LEU | VAL | ||||
| 2 | GLY | VAL | ASN | GLY | LEU | ASP | VAL | THR | SER | LEU | ||||
| 3 | ARG | PRO | PHE | ASP | LEU | VAL | ILE | PRO | PHE | THR | ||||
| 4 | ILE | LYS | LYS | GLY | GLU | ILE | THR | GLY | GLU | VAL | ||||
| 5 | ARG | MET | PRO | SER | GLY | LYS | VAL | ALA | GLN | PRO | ||||
| 6 | THR | ILE | THR | ASP | ASN | LYS | ASP | GLY | THR | VAL | ||||
| 7 | THR | VAL | ARG | TYR | ALA | PRO | SER | GLU | ALA | GLY | ||||
| 8 | LEU | HIS | GLU | MET | ASP | ILE | ARG | TYR | ASP | ASN | ||||
| 9 | MET | HIS | ILE | PRO | GLY | SER | PRO | LEU | GLN | PHE | ||||
| 10 | TYR | VAL | ASP | TYR | VAL | ASN | CYS | GLY | HIS | VAL | ||||
| 11 | THR | ALA | TYR | GLY | PRO | GLY | LEU | THR | HIS | GLY | ||||
| 12 | VAL | VAL | ASN | LYS | PRO | ALA | THR | PHE | THR | VAL | ||||
| 13 | ASN | THR | LYS | ASP | ALA | GLY | GLU | GLY | GLY | LEU | ||||
| 14 | SER | LEU | ALA | ILE | GLU | GLY | PRO | SER | LYS | ALA | ||||
| 15 | GLU | ILE | SER | CYS | THR | ASP | ASN | GLN | ASP | GLY | ||||
| 16 | THR | CYS | SER | VAL | SER | TYR | LEU | PRO | VAL | LEU | ||||
| 17 | PRO | GLY | ASP | TYR | SER | ILE | LEU | VAL | LYS | TYR | ||||
| 18 | ASN | GLU | GLN | HIS | VAL | PRO | GLY | SER | PRO | PHE | ||||
| 19 | THR | ALA | ARG | VAL | THR | GLY | ASP | ASP |
Samples:
sample_1: FLNa16-17, [U-13C; U-15N], 1 mM; sodium phosphate 50 mM; potassium chloride 100 mM; DTT 1 mM; sodium azide 2 mM; EDTA 2 mM; H2O 93%; D2O, [U-100% 2H], 7%
sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 303.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C-CT-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C-CT-HSQC_aromatics | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCDCE)HE | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCD)HD | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
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 600 MHz
- Varian INOVA 800 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts