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- PDB-1f6g: POTASSIUM CHANNEL (KCSA) FULL-LENGTH FOLD -

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Basic information

Entry
Database: PDB / ID: 1f6g
TitlePOTASSIUM CHANNEL (KCSA) FULL-LENGTH FOLD
ComponentsVOLTAGE-GATED POTASSIUM CHANNEL
KeywordsPROTON TRANSPORT / MEMBRANE PROTEIN / POTASSIUM CHANNEL / INTEGRAL MEMBRANE PROTEIN / CYTOPLASMIC DOMAINS
Function / homologyVoltage-gated potassium channel / Potassium channel domain / Ion channel / action potential / voltage-gated potassium channel activity / voltage-gated potassium channel complex / identical protein binding / pH-gated potassium channel KcsA
Function and homology information
Biological speciesStreptomyces lividans (bacteria)
MethodSOLUTION NMR / simulated annealing
AuthorsCortes, D.M. / Perozo, E.
CitationJournal: J.Gen.Physiol. / Year: 2001
Title: Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating.
Authors: Cortes, D.M. / Cuello, L.G. / Perozo, E.
History
DepositionJun 21, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 21, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Data collection / Database references
Category: database_2 / pdbx_nmr_software / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: VOLTAGE-GATED POTASSIUM CHANNEL
B: VOLTAGE-GATED POTASSIUM CHANNEL
C: VOLTAGE-GATED POTASSIUM CHANNEL
D: VOLTAGE-GATED POTASSIUM CHANNEL


Theoretical massNumber of molelcules
Total (without water)70,1424
Polymers70,1424
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)8 / 32structures with the lowest energy
RepresentativeModel #4closest to the average

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Components

#1: Protein
VOLTAGE-GATED POTASSIUM CHANNEL / Coordinate model: Cα atoms only


Mass: 17535.375 Da / Num. of mol.: 4 / Fragment: FULL-LENGTH CHANNEL / Mutation: CYS SCANNING: 5-24, 120-160
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptomyces lividans (bacteria) / Plasmid: PQE32 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A334

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111Power Saturation Experiments in 21% O2 or 10 mM NiEdda
222Dipolar couplings derived from underlabeled samples
NMR detailsText: This structure was determined using secondary structure assignments from frequency analysis of solvent accessibility data and tertiary and quaternary structural information from spin-spin dipolar couplings

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Sample preparation

DetailsContents: 50-100 uM KcsA, PBS pH 7.2, reconstituted into asolectin vesicles at a 1:500 protein:lipid ratio (molar)
Solvent system: 100% H2O
Sample conditionsIonic strength: 50-100 mM / pH: 7.2 / Pressure: ambient / Temperature: 293 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker EMX / Manufacturer: Bruker / Model: EMX / Field strength: 3400 MHz

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Processing

NMR software
NameVersionDeveloperClassification
EPR Aquisit2.32Bruker Instrumentscollection
Discover3MSIstructure solution
Discover3MSIrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: structures are based on a total of 438 restraints, with 84 intra-subunit distance constraints per subunit and 15 inter-subunit constraints
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 32 / Conformers submitted total number: 8

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