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Open data
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Basic information
Entry | Database: PDB / ID: 2lhg | ||||||
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Title | GB98-T25I solution structure | ||||||
![]() | GB98 | ||||||
![]() | DE NOVO PROTEIN | ||||||
Function / homology | Albumin-binding domain / Helicase, Ruva Protein; domain 3 / Orthogonal Bundle / Mainly Alpha![]() | ||||||
Biological species | artificial gene (others) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | He, Y. / Chen, Y. / Alexander, P. / Bryan, P. / Orban, J. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 183.1 KB | Display | ![]() |
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PDB format | ![]() | 152.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 379.5 KB | Display | ![]() |
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Full document | ![]() | 396.4 KB | Display | |
Data in XML | ![]() | 10.1 KB | Display | |
Data in CIF | ![]() | 15.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2lhcC ![]() 2lhdC ![]() 2lheC C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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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: ![]() ![]() |
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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: 7.0 / 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 |