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- PDB-7swj: KirBac1.1 mutant - I131C -

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Basic information

Entry
Database: PDB / ID: 7swj
TitleKirBac1.1 mutant - I131C
ComponentsInward rectifier potassium channelInward-rectifier potassium channel
KeywordsMEMBRANE PROTEIN
Function / homology
Function and homology information


inward rectifier potassium channel activity / monoatomic ion channel complex / metal ion binding
Similarity search - Function
Potassium channel, inwardly rectifying, Kir, cytoplasmic / Potassium channel, inwardly rectifying, Kir / Inward rectifier potassium channel, C-terminal / Inward rectifier potassium channel C-terminal domain / Potassium channel domain / Ion channel / Immunoglobulin E-set
Similarity search - Domain/homology
Inward rectifier potassium channel
Similarity search - Component
Biological speciesBurkholderia pseudomallei (bacteria)
MethodSOLID-STATE NMR / simulated annealing
AuthorsAmani, R. / Wylie, B.J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)1R35GM124979 United States
CitationJournal: Front Mol Biosci / Year: 2021
Title: Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State.
Authors: Amani, R. / Schwieters, C.D. / Borcik, C.G. / Eason, I.R. / Han, R. / Harding, B.D. / Wylie, B.J.
History
DepositionNov 19, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 2, 2022Provider: repository / Type: Initial release
Revision 1.1Feb 23, 2022Group: Structure summary / Category: audit_author / Item: _audit_author.name
Revision 1.2Jun 14, 2023Group: Other / Category: pdbx_database_status / Item: _pdbx_database_status.status_code_nmr_data

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Inward rectifier potassium channel
B: Inward rectifier potassium channel
C: Inward rectifier potassium channel
D: Inward rectifier potassium channel


Theoretical massNumber of molelcules
Total (without water)148,6704
Polymers148,6704
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: assay for oligomerization
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area20780 Å2
ΔGint-153 kcal/mol
Surface area64070 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 800structures with the lowest energy
RepresentativeModel #1target function

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Components

#1: Protein
Inward rectifier potassium channel / Inward-rectifier potassium channel / Inward rectifier potassium channel protein / Potassium channel / Putative inward rectifier potassium channel


Mass: 37167.473 Da / Num. of mol.: 4 / Mutation: I131C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Burkholderia pseudomallei (bacteria) / Gene: BOC38_05990, DF122_01560, X994_2342 / Production host: Escherichia coli M15 (bacteria) / References: UniProt: P83698

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Experimental details

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Experiment

ExperimentMethod: SOLID-STATE NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic1CC2D water edited
121isotropic2CCC3D DARR
131isotropic1NCACX
141isotropic1NCOCX
151isotropic1CANcoCA

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Sample preparation

DetailsType: liposome
Contents: 25 % w/w POPC, 25 % w/w [U-13C; U-15N] KirBac1.1, 100% H2O
Details: protein was reconstituted in 100% POPC lipid bilayer
Label: 15N_13C_sample / Solvent system: 100% H2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
25 % w/wPOPCnatural abundance1
25 % w/wKirBac1.1[U-13C; U-15N]1
Sample conditionsIonic strength: 100 mM / Label: closed state / pH: 7.6 / Pressure: 1 atm / Temperature: 298 K

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NMR measurement

NMR spectrometer
ManufacturerField strength (MHz)Spectrometer-ID
Agilent6001
Agilent7502

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Processing

NMR software
NameVersionDeveloperClassification
NMRFAM-SPARKYMarkleydata analysis
X-PLOR NIH3.2.9Schwieters, Kuszewski, Tjandra and Clorerefinement
X-PLOR NIH3.2.9Schwieters, Kuszewski, Tjandra and Clorestructure calculation
NMRFAM-SPARKYMarkleychemical shift assignment
NMRFAM-SPARKYMarkleypeak picking
RefinementMethod: simulated annealing / Software ordinal: 3
NMR representativeSelection criteria: target function
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 800 / Conformers submitted total number: 10

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