+Open data
-Basic information
Entry | Database: PDB / ID: 2k6a | ||||||
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Title | Solution structure of EAS D15 truncation mutant | ||||||
Components | Hydrophobin | ||||||
Keywords | STRUCTURAL PROTEIN / hydrophobin / EAS / rodlets / assembly / amyloid / Cell wall / Cell wall biogenesis/degradation / Secreted | ||||||
Function / homology | Function and homology information structural constituent of cell wall / fungal-type cell wall / cell wall organization / extracellular region Similarity search - Function | ||||||
Biological species | Neurospora crassa (fungus) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics, molecular dynamics | ||||||
Model details | Solution structure of EAS truncation mutant with 15 residues removed from flexible loop between Cys3 and Cys4 | ||||||
Authors | Kwan, A.H. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2008 Title: The Cys3-Cys4 loop of the hydrophobin EAS is not required for rodlet formation and surface activity. Authors: Kwan, A.H. / Macindoe, I. / Vukasin, P.V. / Morris, V.K. / Kass, I. / Gupte, R. / Mark, A.E. / Templeton, M.D. / Mackay, J.P. / Sunde, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2k6a.cif.gz | 355.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2k6a.ent.gz | 307 KB | Display | PDB format |
PDBx/mmJSON format | 2k6a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k6/2k6a ftp://data.pdbj.org/pub/pdb/validation_reports/k6/2k6a | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 6818.703 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Neurospora crassa (fungus) / Gene: eas, bli-7, ccg-2 / Plasmid: pHUE / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q04571 |
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Sequence details | RESIDUES 15-39 INCLUSIVE HAVE BEEN REMOVED FROM NATIVE EAS (WRT NUMBERING IN EAS) |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: EAS truncation mutant with 15 residues removed from flexible loop between Cys3 and Cys4 | ||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 20 / pH: 6.2 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics, molecular dynamics Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1407 / NOE intraresidue total count: 559 / NOE long range total count: 280 / NOE medium range total count: 74 / NOE sequential total count: 323 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 31 / Protein psi angle constraints total count: 0 | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 500 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0 Å / Maximum torsion angle constraint violation: 5 ° / Maximum upper distance constraint violation: 0.5 Å |