+Open data
-Basic information
Entry | Database: PDB / ID: 2myv | ||||||
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Title | Solution structure of M. oryzae protein AVR1-CO39 | ||||||
Components | Uncharacterized protein | ||||||
Keywords | UNKNOWN FUNCTION | ||||||
Function / homology | Uncharacterized protein Function and homology information | ||||||
Biological species | Magnaporthe grisea (fungus) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, molecular dynamics | ||||||
Model details | lowest energy, model1 | ||||||
Authors | de Guillen, K. / Kroj, T. | ||||||
Citation | Journal: Plos Pathog. / Year: 2015 Title: Structure Analysis Uncovers a Highly Diverse but Structurally Conserved Effector Family in Phytopathogenic Fungi. Authors: de Guillen, K. / Ortiz-Vallejo, D. / Gracy, J. / Fournier, E. / Kroj, T. / Padilla, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2myv.cif.gz | 480.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2myv.ent.gz | 402.9 KB | Display | PDB format |
PDBx/mmJSON format | 2myv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2myv_validation.pdf.gz | 542.6 KB | Display | wwPDB validaton report |
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Full document | 2myv_full_validation.pdf.gz | 740.6 KB | Display | |
Data in XML | 2myv_validation.xml.gz | 34.4 KB | Display | |
Data in CIF | 2myv_validation.cif.gz | 54.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/my/2myv ftp://data.pdbj.org/pub/pdb/validation_reports/my/2myv | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11243.166 Da / Num. of mol.: 1 / Fragment: residues 22-89 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Magnaporthe grisea (fungus) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 DE3 / References: UniProt: Q8J180 |
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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: 0.15 / pH: 6.8 / Pressure: ambient / Temperature: 305 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1286 / NOE long range total count: 384 / NOE medium range total count: 157 / Hydrogen bond constraints total count: 30 | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 20 / Maximum torsion angle constraint violation: 4 ° / Maximum upper distance constraint violation: 0.3 Å |