Structure of human KCNE1 (also known as MinK) in LMPG micelles. KCNE1 modulates certain voltage- ...Structure of human KCNE1 (also known as MinK) in LMPG micelles. KCNE1 modulates certain voltage-gated potassium channels.
Mass: 15706.869 Da / Num. of mol.: 1 / Mutation: R104K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KCNE1 / Plasmid: pET16b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) codon plus RP / References: UniProt: Q6FHJ6, UniProt: P15382*PLUS
Sequence details
THESE COORDINATES ARE FOR THE R104K MUTANT FORM OF KCNE1, WHICH WAS GENERATED AT AN EARLY STAGE IN ...THESE COORDINATES ARE FOR THE R104K MUTANT FORM OF KCNE1, WHICH WAS GENERATED AT AN EARLY STAGE IN STRUCTURAL DETERMINATION BY A PCR ERROR. THE R104K MUTANT MODULATES KCNQ1 CHANNEL FUNCTION IN WILD TYPE-LIKE MANNER. MUTATION OF THIS ARG RESIDUE TO LYS IS OBSERVED IN MAMMALIAN KCNE1 HOMOLOGS TO THE HUMAN PROTEIN.
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
2D TROSY-1H-15N HSQC
1
2
2
3D TROSY-HNCO
1
3
2
3D TROSY-HNCA
1
4
2
3D TROSY-HN(CO)CA
1
5
2
3D TROSY-CBCA(CO)NH
1
6
2
3D TROSY-HN(CA)CB
1
7
3
3D 1H-15N TROSY-NOESY
1
8
4
2D TROSY-1H-15N HSQC
NMR details
Text: The structure was determined using combination of NOEs, PREs, and RDCs.
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
0.5-1 mM [U-100% 15N] KCNE1 (MinK), 10 % D2O, 2 mM EDTA, 2 mM DTT, 250 mM imidazole, 4 % LMPG, 90% H2O/10% D2O
90% H2O/10% D2O
2
1 mM [U-13C; U-15N; U-2H] KCNE1 (MinK), 10 % D2O, 2 mM EDTA, 2 mM DTT, 250 mM imidazole, 4 % LMPG, 90% H2O/10% D2O
90% H2O/10% D2O
3
1 mM [U-100% 13C; U-100% 15N; 70% 2H] KCNE1 (MinK), 10 % D2O, 2 mM EDTA, 2 mM DTT, 250 mM imidazole, 4 % LMPG, 90% H2O/10% D2O
90% H2O/10% D2O
4
1 mM [U-15N; U-2H] KCNE1 (MinK), 10 % D2O, 2 mM EDTA, 2 mM DTT, 250 mM imidazole, 4 % LMPG, 90% H2O/10% D2O
Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 Details: The refinement protocol consisted of slow cooling from 1000 K to 100 K spanning 45 ps. Final structures were energy-minimized using 250 steps of Powell energy minimization. The 20 structures ...Details: The refinement protocol consisted of slow cooling from 1000 K to 100 K spanning 45 ps. Final structures were energy-minimized using 250 steps of Powell energy minimization. The 20 structures with lowest energy were subjected to further analysis and spin-labeled Cys residues associated with PRE restraints were changed back to their wild type residues. Powell energy minimization was then performed.
NMR constraints
NOE constraints total: 737 / NOE intraresidue total count: 126 / NOE long range total count: 464 / NOE medium range total count: 50 / NOE sequential total count: 97 / Hydrogen bond constraints total count: 72 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 113 / Protein psi angle constraints total count: 112
NMR representative
Selection criteria: closest to the average
NMR ensemble
Average torsion angle constraint violation: 0.2 ° Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 500 / Conformers submitted total number: 10 / Maximum lower distance constraint violation: 0.137 Å / Maximum torsion angle constraint violation: 4.569 ° / Maximum upper distance constraint violation: 0.129 Å / Torsion angle constraint violation method: XPLOR
NMR ensemble rms
Distance rms dev: 0.008 Å / Distance rms dev error: 0.0019 Å
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