- PDB-1n7l: Solution NMR structure of phospholamban in detergent micelles -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 1n7l
Title
Solution NMR structure of phospholamban in detergent micelles
Components
Cardiac phospholamban
Keywords
SIGNALING PROTEIN / helix-turn-helix
Function / homology
Function and homology information
negative regulation of calcium ion binding / negative regulation of calcium ion import into sarcoplasmic reticulum / negative regulation of ATPase-coupled calcium transmembrane transporter activity / adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / regulation of relaxation of muscle / regulation of the force of heart contraction by cardiac conduction / calcium ion-transporting ATPase complex / acrosome assembly / negative regulation of calcium ion transmembrane transporter activity / negative regulation of calcium ion import ...negative regulation of calcium ion binding / negative regulation of calcium ion import into sarcoplasmic reticulum / negative regulation of ATPase-coupled calcium transmembrane transporter activity / adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process / regulation of relaxation of muscle / regulation of the force of heart contraction by cardiac conduction / calcium ion-transporting ATPase complex / acrosome assembly / negative regulation of calcium ion transmembrane transporter activity / negative regulation of calcium ion import / negative regulation of catalytic activity / ATPase inhibitor activity / cardiac muscle tissue development / regulation of cardiac muscle cell contraction / enzyme inhibitor activity / negative regulation of heart rate / muscle cell cellular homeostasis / regulation of calcium ion transport / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / Notch signaling pathway / sarcoplasmic reticulum membrane / mitochondrial membrane / intracellular calcium ion homeostasis / ATPase binding / endoplasmic reticulum membrane / perinuclear region of cytoplasm / endoplasmic reticulum / protein homodimerization activity / identical protein binding Similarity search - Function
Phospholamban / Phospholamban / Phospholamban / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha Similarity search - Domain/homology
structures with acceptable covalent geometry,structures with the least restraint violations,structures with the lowest energy
Representative
Model #15
fewest violations
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Components
#1: Protein
Cardiacphospholamban / PLB
Mass: 6150.477 Da / Num. of mol.: 1 / Mutation: C37A C42F C47A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Gene: PLN / Plasmid: pMAL / Production host: Escherichia coli (E. coli) / Strain (production host): BL21DE3phi / References: UniProt: P61015
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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 15N-separated NOESY
1
2
1
3D 15N-separated TOCSY
1
3
1
HNCA
1
4
1
HN(CO)CA
1
5
1
HN(CA)CB
1
6
1
HNCO
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Sample preparation
Details
Contents: 1 mM phospholamban U-15N,13C; 20 mM phosphate buffer; 90% H2O, 10% D2O; pH=4.2; 600 mM DPC;
Sample conditions
pH: 4.2 / Pressure: 1 atm / Temperature: 323 K
Crystal grow
*PLUS
Method: other / Details: NMR
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NMR measurement
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelength
Relative weight: 1
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Varian INOVA
Varian
INOVA
800
1
Varian INOVA
Varian
INOVA
600
2
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Processing
NMR software
Name
Version
Developer
Classification
VNMR
Varian
collection
NMRPipe
FrankDelaglio
processing
NMRView
5
BruceA. Johnson
dataanalysis
XPLOR-NIH
2.0.4
G. MariusClore , JohnKuszewski, CharlesD. Schwieters, andNicoTjandra
structuresolution
XPLOR-NIH
2.0.4
Clore
refinement
Refinement
Method: simulated annealing / Software ordinal: 1
NMR representative
Selection criteria: fewest violations
NMR ensemble
Conformer selection criteria: structures with acceptable covalent geometry,structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20
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