+Open data
-Basic information
Entry | Database: PDB / ID: 2hm5 | ||||||
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Title | NW1, K21P, Structural Species II | ||||||
Components | Nematocyst outer wall antigen | ||||||
Keywords | STRUCTURAL PROTEIN / molecular evolution / nematocyst / bridge state / cysteine rich | ||||||
Function / homology | Function and homology information Golgi-associated plant pathogenesis-related protein 1, SCP domain / SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains. / CAP domain / CAP superfamily / Cysteine-rich secretory protein family / SEA domain / SEA domain / Lectin C-type domain / C-type lectin domain profile. / C-type lectin-like ...Golgi-associated plant pathogenesis-related protein 1, SCP domain / SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains. / CAP domain / CAP superfamily / Cysteine-rich secretory protein family / SEA domain / SEA domain / Lectin C-type domain / C-type lectin domain profile. / C-type lectin-like / C-type lectin (CTL) or carbohydrate-recognition domain (CRD) / C-type lectin-like/link domain superfamily / C-type lectin fold Similarity search - Domain/homology | ||||||
Biological species | Hydra vulgaris (swiftwater hydra) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Meier, S. / Jensen, P.R. / Grzesiek, S. / Oezbek, S. | ||||||
Citation | Journal: Curr.Biol. / Year: 2007 Title: Continuous molecular evolution of protein-domain structures by single amino Acid changes. Authors: Meier, S. / Jensen, P.R. / David, C.N. / Chapman, J. / Holstein, T.W. / Grzesiek, S. / Ozbek, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2hm5.cif.gz | 71.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2hm5.ent.gz | 56.7 KB | Display | PDB format |
PDBx/mmJSON format | 2hm5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hm/2hm5 ftp://data.pdbj.org/pub/pdb/validation_reports/hm/2hm5 | HTTPS FTP |
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-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/peptide | Mass: 3048.367 Da / Num. of mol.: 1 / Fragment: NW1 / Mutation: K21P Source method: isolated from a genetically manipulated source Source: (gene. exp.) Hydra vulgaris (swiftwater hydra) / Gene: NOWA / Production host: Escherichia coli (E. coli) / References: UniProt: Q8IT70 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.6 mM NW1 K21P II, 5 mM phosphate buffer, 95% H2O, 5% D2O Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 10 mM / pH: 5.5 / Pressure: ambient / Temperature: 288 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |