+
Open data
-
Basic information
Entry | Database: PDB / ID: 2k9u | ||||||
---|---|---|---|---|---|---|---|
Title | Solution NMR structure of the Filamin-migfilin complex | ||||||
![]() |
| ||||||
![]() | STRUCTURAL PROTEIN / cytoskeletal complex / Cell adhesion / Cell junction / Cell shape / Cytoskeleton / LIM domain / Metal-binding | ||||||
Function / homology | ![]() regulation of integrin activation / filamin binding / Cell-extracellular matrix interactions / costamere / ankyrin binding / intercellular bridge / sarcomere organization / sarcoplasm / stress fiber / cytoskeletal protein binding ...regulation of integrin activation / filamin binding / Cell-extracellular matrix interactions / costamere / ankyrin binding / intercellular bridge / sarcomere organization / sarcoplasm / stress fiber / cytoskeletal protein binding / cell periphery / sarcolemma / fibrillar center / Z disc / cell-cell adhesion / actin filament binding / cell junction / regulation of cell shape / cytoskeleton / focal adhesion / identical protein binding / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Ithychanda, S.N. / Qin, J. | ||||||
![]() | ![]() Title: Migfilin, a molecular switch in regulation of integrin activation. Authors: Ithychanda, S.S. / Das, M. / Ma, Y.Q. / Ding, K. / Wang, X. / Gupta, S. / Wu, C. / Plow, E.F. / Qin, J. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 921.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 787.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 351.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 623.9 KB | Display | |
Data in XML | ![]() | 72.8 KB | Display | |
Data in CIF | ![]() | 95.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 12434.720 Da / Num. of mol.: 1 / Fragment: UNP residues 919-1032 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Protein/peptide | Mass: 2661.150 Da / Num. of mol.: 1 / Fragment: UNP residues 1-24 / Source method: obtained synthetically Details: Synthetic peptide of the sequence corresponding to residues 1-24 of human Filamin-binding LIM protein 1, UniProt entry Q8WUP2, FBLI1_HUMAN References: UniProt: Q8WUP2 |
Sequence details | THE N-TERMINAL RESIDUES GIPEF ARE THE EXPRESSION |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|---|
NMR experiment | Type: 3D HN(CA)CB |
-
Sample preparation
Details | Contents: 0.1-1 mM [U-100% 13C; U-100% 15N] entity_1, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample | Units: mM / Component: entity_1 / Isotopic labeling: [U-100% 13C; U-100% 15N] / Conc. range: 0.1-1 |
Sample conditions | Ionic strength: 0.025 / pH: 6.4 / Pressure: ambient / Temperature: 302 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
---|
-
Processing
NMR software |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 Details: 1. The regions 1-15 and 109-119 of entity 1 (chain A), because they are not part of Ig (immunoglobulin-like) domain, have few contraints and are essentially unfolded. 2. In entity 2 (chain B ...Details: 1. The regions 1-15 and 109-119 of entity 1 (chain A), because they are not part of Ig (immunoglobulin-like) domain, have few contraints and are essentially unfolded. 2. In entity 2 (chain B peptide), the regions 1-6 and 18-24 do not have many constraints and seem unfolded. | |||||||||
NMR representative | Selection criteria: lowest energy | |||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 30 / Conformers submitted total number: 20 |