+Open data
-Basic information
Entry | Database: PDB / ID: 2lhg | ||||||
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Title | GB98-T25I solution structure | ||||||
Components | GB98 | ||||||
Keywords | DE NOVO PROTEIN | ||||||
Function / homology | Albumin-binding domain / Helicase, Ruva Protein; domain 3 / Orthogonal Bundle / Mainly Alpha Function and homology information | ||||||
Biological species | artificial gene (others) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | He, Y. / Chen, Y. / Alexander, P. / Bryan, P. / Orban, J. | ||||||
Citation | Journal: Structure / Year: 2012 Title: Mutational tipping points for switching protein folds and functions. Authors: He, Y. / Chen, Y. / Alexander, P.A. / Bryan, P.N. / Orban, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lhg.cif.gz | 183.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lhg.ent.gz | 152.1 KB | Display | PDB format |
PDBx/mmJSON format | 2lhg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2lhg_validation.pdf.gz | 379.5 KB | Display | wwPDB validaton report |
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Full document | 2lhg_full_validation.pdf.gz | 396.4 KB | Display | |
Data in XML | 2lhg_validation.xml.gz | 10.1 KB | Display | |
Data in CIF | 2lhg_validation.cif.gz | 15.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lh/2lhg ftp://data.pdbj.org/pub/pdb/validation_reports/lh/2lhg | HTTPS FTP |
-Related structure data
Related structure data | 2lhcC 2lhdC 2lheC C: citing same article (ref.) |
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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: 6417.416 Da / Num. of mol.: 1 / Mutation: T25I Source method: isolated from a genetically manipulated source Source: (gene. exp.) artificial gene (others) / Gene: PGB98 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21DE3 |
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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: 0.1-0.3 mM [U-100% 13C; U-100% 15N] GB98-T25I, 100 mM potassium phosphate, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 100 / pH: 7 / Pressure: ambient / Temperature: 278 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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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: 3000 / Conformers submitted total number: 10 |