BMRB Entry 30958
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30958
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Title: Filamin complex-2
Deposition date: 2021-10-04 Original release date: 2023-04-04
Authors: Liu, J.; Qin, J.
Citation: Liu, J.; Qin, J.. "Filamin complex-2" .
Assembly members:
entity_1, polymer, 95 residues, 9762.721 Da.
entity_2, polymer, 21 residues, 2581.789 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 phage EcSzw-2
Entity Sequences (FASTA):
entity_1: GGAHKVRAGGPGLERAEAGV
PAEFSIWTREAGAGGLAIAV
EGPSKAEISFEDRKDGSCGV
AYVVQEPGDYEVSVKFNEEH
IPDSPFVVPVASPSG
entity_2: WKVGFFKRNRPPLEEDDEEG
E
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 167 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 550 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 2 |
Entities:
Entity 1, unit_1 95 residues - 9762.721 Da.
| 1 | GLY | GLY | ALA | HIS | LYS | VAL | ARG | ALA | GLY | GLY | ||||
| 2 | PRO | GLY | LEU | GLU | ARG | ALA | GLU | ALA | GLY | VAL | ||||
| 3 | PRO | ALA | GLU | PHE | SER | ILE | TRP | THR | ARG | GLU | ||||
| 4 | ALA | GLY | ALA | GLY | GLY | LEU | ALA | ILE | ALA | VAL | ||||
| 5 | GLU | GLY | PRO | SER | LYS | ALA | GLU | ILE | SER | PHE | ||||
| 6 | GLU | ASP | ARG | LYS | ASP | GLY | SER | CYS | GLY | VAL | ||||
| 7 | ALA | TYR | VAL | VAL | GLN | GLU | PRO | GLY | ASP | TYR | ||||
| 8 | GLU | VAL | SER | VAL | LYS | PHE | ASN | GLU | GLU | HIS | ||||
| 9 | ILE | PRO | ASP | SER | PRO | PHE | VAL | VAL | PRO | VAL | ||||
| 10 | ALA | SER | PRO | SER | GLY |
Entity 2, unit_2 21 residues - 2581.789 Da.
| 1 | TRP | LYS | VAL | GLY | PHE | PHE | LYS | ARG | ASN | ARG | ||||
| 2 | PRO | PRO | LEU | GLU | GLU | ASP | ASP | GLU | GLU | GLY | ||||
| 3 | GLU |
Samples:
sample_1: filamin Ig21, [U-100% 13C; U-100% 15N], 1 mM; Integrin alpha-IIb light chain 2 mM
sample_2: filamin Ig21, [U-15N; U-2H], 1 mM; Integrin alpha-IIb light chain 2 mM
sample_3: Integrin alpha-IIb light chain 2 mM; GST-filamin-Ig21 0.05 mM
sample_conditions_1: ionic strength: 61 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_3 | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - collection
Sparky, Goddard - chemical shift assignment, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMR spectrometers:
- Bruker AVANCE 600 MHz
- Bruker AVANCE 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts