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- PDB-2nbs: Backbone 1H, 13C, and 15N Chemical Shift Assignments for designed... -

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Basic information

Entry
Database: PDB / ID: 2nbs
TitleBackbone 1H, 13C, and 15N Chemical Shift Assignments for designed protein E_1r26
ComponentsE_1r26
KeywordsUNKNOWN FUNCTION / designed protein
Function / homologyGlutaredoxin / Glutaredoxin / 3-Layer(aba) Sandwich / Alpha Beta
Function and homology information
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model1
AuthorsZhou, X.
CitationJournal: To be Published
Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for designed protein E_1r26
Authors: Zhou, X.
History
DepositionMar 12, 2016Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Oct 19, 2016Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: E_1r26


Theoretical massNumber of molelcules
Total (without water)13,9911
Polymers13,9911
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 1000structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein E_1r26


Mass: 13990.840 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli)

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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 C(CO)NH
1413D HN(CA)CB
1513D CBCA(CO)NH
1613D HBHA(CO)NH
1713D HN(CO)CA
1813D H(CCO)NH
1913D 1H-13C NOESY
11013D 1H-15N TOCSY

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Sample preparation

DetailsContents: 0.02mM sodium phosphate-1, 0.01mM EDTA-2, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentSolution-ID
0.02 mMsodium phosphate-11
0.01 mMEDTA-21
Sample conditionsIonic strength: 0.05 / pH: 6.5 / Pressure: ambient / Temperature: 298 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
NameDeveloperClassification
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
CYANArefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 1000 / Conformers submitted total number: 20 / Representative conformer: 1

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