BMRB Entry 25176
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25176
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Title: The structure of Filamin repeat 21 bound to integrin
Deposition date: 2014-08-28 Original release date: 2015-03-20
Authors: Liu, Jianmin; Qin, Jun
Citation: Liu, Jianmin; Das, Mitali; Yang, Jun; Ithychanda, Sujay; Yakubenko, Valentin; Plow, Edward; Qin, Jun. "Structural mechanism of integrin inactivation by filamin" Nat. Struct. Mol. Biol. ., .-. (2015).
Assembly members:
entity_1, polymer, 95 residues, 9762.817 Da.
entity_2, polymer, 21 residues, 2581.817 Da.
entity_3, polymer, 47 residues, 5618.380 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: GGAHKVRAGGPGLERAEAGV
PAEFSIWTREAGAGGLAIAV
EGPSKAEISFEDRKDGSCGV
AYVVQEPGDYEVSVKFNEEH
IPDSPFVVPVASPSG
entity_2: WKVGFFKRNRPPLEEDDEEG
E
entity_3: KKKITIHDRKEFAKFEEERA
RAKWDTANNPLYKEATSTFT
NITYRGT
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 897 |
| 13C chemical shifts | 400 |
| 15N chemical shifts | 133 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
| 3 | entity_3 | 3 |
Entities:
Entity 1, entity_1 95 residues - 9762.817 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, entity_2 21 residues - 2581.817 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 |
Entity 3, entity_3 47 residues - 5618.380 Da.
| 1 | LYS | LYS | LYS | ILE | THR | ILE | HIS | ASP | ARG | LYS | ||||
| 2 | GLU | PHE | ALA | LYS | PHE | GLU | GLU | GLU | ARG | ALA | ||||
| 3 | ARG | ALA | LYS | TRP | ASP | THR | ALA | ASN | ASN | PRO | ||||
| 4 | LEU | TYR | LYS | GLU | ALA | THR | SER | THR | PHE | THR | ||||
| 5 | ASN | ILE | THR | TYR | ARG | GLY | THR |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM; entity_2, [U-100% 13C; U-100% 15N; U-80% 2H], mM; entity_3, [U-100% 13C; U-100% 15N; U-80% 2H], mM; H2O 90%; D2O 10%
sample_conditions_1: temperature: 298 K; pH: 6.4; pressure: 1 atm; ionic strength: 25 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
SPARKY: Backbone
or all simulated shifts