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- PDB-2lhg: GB98-T25I solution structure -

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Basic information

Entry
Database: PDB / ID: 2lhg
TitleGB98-T25I solution structure
ComponentsGB98
KeywordsDE NOVO PROTEIN
Function / homologyAlbumin-binding domain / Helicase, Ruva Protein; domain 3 / Orthogonal Bundle / Mainly Alpha
Function and homology information
Biological speciesartificial gene (others)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model 1
AuthorsHe, Y. / Chen, Y. / Alexander, P. / Bryan, P. / Orban, J.
CitationJournal: 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
DepositionAug 8, 2011Deposition site: BMRB / Processing site: RCSB
Revision 1.0Feb 29, 2012Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GB98


Theoretical massNumber of molelcules
Total (without water)6,4171
Polymers6,4171
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 3000structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein GB98


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

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1213D CBCA(CO)NH
1313D HNCO
1413D 1H-15N NOESY
1513D HNCA

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Sample preparation

DetailsContents: 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
Sample
Conc. (mg/ml)UnitsComponentIsotopic labelingConc. range (mg/ml)Solution-ID
mMGB98-T25I-1[U-100% 13C; U-100% 15N]0.1-0.31
100 mMpotassium phosphate-21
Sample conditionsIonic strength: 100 / pH: 7.0 / Pressure: ambient / Temperature: 278 K

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NMR measurement

NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CS_ROSETTA3.XYang Shen, Oliver Lange, Frank Delaglio, et al.data analysis
CS_ROSETTA3.XYang Shen, Oliver Lange, Frank Delaglio, et al.refinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 3000 / Conformers submitted total number: 10

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