+Open data
-Basic information
Entry | Database: PDB / ID: 1qqv | ||||||
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Title | SOLUTION STRUCTURE OF THE HEADPIECE DOMAIN OF CHICKEN VILLIN | ||||||
Components | VILLIN HEADPIECE DOMAINVillin-1 | ||||||
Keywords | STRUCTURAL PROTEIN / F-ACTIN BINDING DOMAIN / SALT-BRIDGE | ||||||
Function / homology | Function and homology information regulation of actin nucleation / cytoplasmic actin-based contraction involved in cell motility / lysophosphatidic acid binding / regulation of lamellipodium morphogenesis / filopodium tip / positive regulation of actin filament bundle assembly / actin filament severing / regulation of wound healing / actin filament capping / barbed-end actin filament capping ...regulation of actin nucleation / cytoplasmic actin-based contraction involved in cell motility / lysophosphatidic acid binding / regulation of lamellipodium morphogenesis / filopodium tip / positive regulation of actin filament bundle assembly / actin filament severing / regulation of wound healing / actin filament capping / barbed-end actin filament capping / actin polymerization or depolymerization / actin filament depolymerization / cellular response to hepatocyte growth factor stimulus / positive regulation of epithelial cell migration / actin filament bundle / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / microvillus / cellular response to epidermal growth factor stimulus / ruffle / phosphatidylinositol-4,5-bisphosphate binding / actin filament polymerization / filopodium / response to bacterium / epidermal growth factor receptor signaling pathway / actin filament binding / actin cytoskeleton / lamellipodium / regulation of cell shape / positive regulation of cell migration / calcium ion binding / protein homodimerization activity / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY SIMULATED ANNEALING | ||||||
Model type details | minimized average | ||||||
Authors | Vardar, D. / Buckley, D.A. / Frank, B.S. / McKnight, C.J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 Title: NMR structure of an F-actin-binding "headpiece" motif from villin. Authors: Vardar, D. / Buckley, D.A. / Frank, B.S. / McKnight, C.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qqv.cif.gz | 29.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qqv.ent.gz | 23.2 KB | Display | PDB format |
PDBx/mmJSON format | 1qqv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qq/1qqv ftp://data.pdbj.org/pub/pdb/validation_reports/qq/1qqv | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7611.663 Da / Num. of mol.: 1 / Fragment: HP67 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: P02640 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The coordinates are the average of the 10 lowest energy structures of the 31 calculated. |
-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY SIMULATED ANNEALING / Software ordinal: 1 Details: THIS MINIMIZED AVERAGE STRUCTURE BASED ON A TOTAL OF 1219 DISTANCE RESTRAINTS, 1201 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 18 ARE FROM HYDROGEN BONDS. THERE ARE 61 DIHEDRAL ANGLE RESTRAINTS. | |||||||||
NMR representative | Selection criteria: minimized average structure | |||||||||
NMR ensemble | Conformer selection criteria: no NOE violation > 0.3, no angle violations greater than 5 degrees Conformers calculated total number: 31 / Conformers submitted total number: 1 |