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Yorodumi- PDB-2n4o: Solution structure of the hydrophobin MPG1 from the rice blast fu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2n4o | ||||||
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Title | Solution structure of the hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae | ||||||
Components | Hydrophobin-like protein MPG1 | ||||||
Keywords | STRUCTURAL PROTEIN / amyloid | ||||||
Function / homology | Fungal hydrophobin / Hydrophobin, conserved site / Fungal hydrophobins signature. / Hydrophobin / Hydrophobins / structural constituent of cell wall / fungal-type cell wall / extracellular region / Hydrophobin-like protein MPG1 Function and homology information | ||||||
Biological species | Magnaporthe oryzae 70-15 (fungus) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Rey, A.A. / Kwan, A.H. / Sunde, M. | ||||||
Citation | Journal: Sci Rep / Year: 2016 Title: Self-assembly of MPG1, a hydrophobin protein from the rice blast fungus that forms functional amyloid coatings, occurs by a surface-driven mechanism. Authors: Pham, C.L. / Rey, A. / Lo, V. / Soules, M. / Ren, Q. / Meisl, G. / Knowles, T.P. / Kwan, A.H. / Sunde, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n4o.cif.gz | 527.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n4o.ent.gz | 444.7 KB | Display | PDB format |
PDBx/mmJSON format | 2n4o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n4/2n4o ftp://data.pdbj.org/pub/pdb/validation_reports/n4/2n4o | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 9869.354 Da / Num. of mol.: 1 / Fragment: residues 19-112 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Magnaporthe oryzae 70-15 (fungus) / Strain: 70-15 / ATCC MYA-4617 / FGSC 8958 / Gene: MGCH7_ch7g1089, MGG_10315, MPG1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P52751 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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: 50 / pH: 5.5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1384 / NOE intraresidue total count: 526 / NOE long range total count: 222 / NOE medium range total count: 154 / NOE sequential total count: 407 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 67 / Protein psi angle constraints total count: 67 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 upper distance constraint violation: 0.5 Å |