- PDB-1c17: A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 1c17
Title
A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE
Components
ATP SYNTHASE SUBUNIT A
ATP SYNTHASE SUBUNIT C
Keywords
MEMBRANE PROTEIN / HELIX / COMPLEX
Function / homology
Function and homology information
proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / lipid binding / plasma membrane Similarity search - Function
ATP synthase, F0 complex, subunit A / F1F0 ATP synthase subunit C / F1FO ATP Synthase / ATP synthase, F0 complex, subunit A, bacterial/chloroplast / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / ATP synthase, F0 complex, subunit A / ATP synthase, F0 complex, subunit A, active site / ATP synthase, F0 complex, subunit A superfamily / ATP synthase A chain / ATP synthase a subunit signature. ...ATP synthase, F0 complex, subunit A / F1F0 ATP synthase subunit C / F1FO ATP Synthase / ATP synthase, F0 complex, subunit A, bacterial/chloroplast / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / ATP synthase, F0 complex, subunit A / ATP synthase, F0 complex, subunit A, active site / ATP synthase, F0 complex, subunit A superfamily / ATP synthase A chain / ATP synthase a subunit signature. / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / Four Helix Bundle (Hemerythrin (Met), subunit A) / Up-down Bundle / Mainly Alpha Similarity search - Domain/homology
A: ATP SYNTHASE SUBUNIT C B: ATP SYNTHASE SUBUNIT C C: ATP SYNTHASE SUBUNIT C D: ATP SYNTHASE SUBUNIT C E: ATP SYNTHASE SUBUNIT C F: ATP SYNTHASE SUBUNIT C G: ATP SYNTHASE SUBUNIT C H: ATP SYNTHASE SUBUNIT C I: ATP SYNTHASE SUBUNIT C J: ATP SYNTHASE SUBUNIT C K: ATP SYNTHASE SUBUNIT C L: ATP SYNTHASE SUBUNIT C M: ATP SYNTHASE SUBUNIT A
Mass: 8259.064 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P68699
#2: Protein
ATPSYNTHASESUBUNITA
Mass: 19869.004 Da / Num. of mol.: 1 / Fragment: CONSENSUS HELICES OF SUBUNIT A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P0AB98
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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
3D 13C-SEPARATED NOESY
1
2
1
3D 15N-SEPARATED NOESY
2
3
1
3D 13C-SEPARATED NOESY
2
4
1
3D 15N-SEPARATED NOESY
NMR details
Text: THE STRUCTURES OF SUBUNIT C MONOMERS WERE DETERMINED BY TRIPLE RESONANCE TECHNIQUES THE MODELS OF SUBUNIT A, THE C12 SUBCOMPLEX, AND THE AC12 SUBCOMPLEX USED DISLUFIDE CROSS-LINKS AS ...Text: THE STRUCTURES OF SUBUNIT C MONOMERS WERE DETERMINED BY TRIPLE RESONANCE TECHNIQUES THE MODELS OF SUBUNIT A, THE C12 SUBCOMPLEX, AND THE AC12 SUBCOMPLEX USED DISLUFIDE CROSS-LINKS AS CONSTRAINTS IN CONJUCNTION WITH THE NMR SOLUTION STRUCTURES OF SUBUNIT C
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Sample preparation
Details
Contents: 1 MM SUBUNIT C
Sample conditions
Conditions-ID
Ionic strength
pH
Pressure (kPa)
Temperature (K)
1
50mM
5.0
AMBIENT
300K
2
50mM
8.0
AMBIENT
300K
Crystal grow
*PLUS
Method: other / Details: NMR
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NMR measurement
NMR spectrometer
Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz
Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 20 / Conformers submitted total number: 1
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