CHAPERONE / cataract-causing heat shock protein alpha-crystallin B Chain beta sandwich
Function / homology
Function and homology information
microtubule polymerization or depolymerization / negative regulation of intracellular transport / apoptotic process involved in morphogenesis / cardiac myofibril / regulation of programmed cell death / tubulin complex assembly / structural constituent of eye lens / negative regulation of amyloid fibril formation / M band / lens development in camera-type eye ...microtubule polymerization or depolymerization / negative regulation of intracellular transport / apoptotic process involved in morphogenesis / cardiac myofibril / regulation of programmed cell death / tubulin complex assembly / structural constituent of eye lens / negative regulation of amyloid fibril formation / M band / lens development in camera-type eye / muscle organ development / actin filament bundle / HSF1-dependent transactivation / negative regulation of reactive oxygen species metabolic process / negative regulation of protein-containing complex assembly / stress-activated MAPK cascade / synaptic membrane / muscle contraction / response to hydrogen peroxide / negative regulation of cell growth / cellular response to gamma radiation / Z disc / unfolded protein binding / protein folding / response to estradiol / amyloid-beta binding / response to heat / protein refolding / microtubule binding / perikaryon / dendritic spine / lysosome / protein stabilization / response to hypoxia / axon / negative regulation of gene expression / negative regulation of DNA-templated transcription / protein-containing complex binding / negative regulation of apoptotic process / structural molecule activity / cell surface / protein homodimerization activity / protein-containing complex / mitochondrion / extracellular exosome / nucleoplasm / identical protein binding / nucleus / metal ion binding / cytoplasm / cytosol Similarity search - Function
Alpha-crystallin B chain, ACD domain / Alpha-crystallin, N-terminal / Alpha crystallin A chain, N terminal / Alpha crystallin/Small heat shock protein, animal type / Hsp20/alpha crystallin family / Small heat shock protein (sHSP) domain profile. / Alpha crystallin/Hsp20 domain / HSP20-like chaperone Similarity search - Domain/homology
Mass: 10099.370 Da / Num. of mol.: 2 / Mutation: R120G Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CRYAB, CRYA2, HSPB5 / Production host: Escherichia coli (E. coli) / References: UniProt: P02511
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Sample state
Spectrometer-ID
Type
1
1
1
isotropic
4
3D NOESY
1
2
2
isotropic
2
3D HNCA
1
3
3
isotropic
2
3D HNCA
1
4
1
isotropic
2
3D HNCO
1
5
3
isotropic
2
3D HN(CA)CB
1
6
3
isotropic
2
3DHN(COCA)CB
1
7
3
isotropic
2
3DHN(CO)CA
1
8
1
isotropic
5
3D (H)CCH-TOCSY
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Sample preparation
Details
Type
Solution-ID
Contents
Label
Solvent system
solution
1
1 mM [U-13C; U-15N] HSPB5 mutant R120G-ACD, 50 mM no label sodium phosphate, 100 mM no label sodium chloride, 100 uM no label EDTA, 1 mM no label PMSF, 90% H2O/10% D2O
13C_15N_sample
90% H2O/10% D2O
solution
2
1 mM [U-13C; U-15N; 50%-2H] HSPB5 mutant R120G-ACD, 50 mM no label sodium phosphate, 100 mM no label sodium chloride, 100 uM no label EDTA, 1 mM no label PMSF, 90% H2O/10% D2O
13C15N2H_50sample
90% H2O/10% D2O
solution
3
1 mM [U-13C; U-15N; U-2H] HSPB5 mutant R120G-ACD, 50 mM no label sodium phosphate, 100 mM no label sodium chloride, 100 uM no label EDTA, 1 mM no label PMSF, 90% H2O/10% D2O
13C15N2H_sample
90% H2O/10% D2O
Sample
Conc. (mg/ml)
Component
Isotopic labeling
Solution-ID
1mM
HSPB5 mutant R120G-ACD
[U-13C; U-15N]
1
50mM
sodiumphosphate
nolabel
1
100mM
sodiumchloride
nolabel
1
100uM
EDTA
nolabel
1
1mM
PMSF
nolabel
1
1mM
HSPB5 mutant R120G-ACD
[U-13C; U-15N; 50%-2H]
2
50mM
sodiumphosphate
nolabel
2
100mM
sodiumchloride
nolabel
2
100uM
EDTA
nolabel
2
1mM
PMSF
nolabel
2
1mM
HSPB5 mutant R120G-ACD
[U-13C; U-15N; U-2H]
3
50mM
sodiumphosphate
nolabel
3
100mM
sodiumchloride
nolabel
3
100uM
EDTA
nolabel
3
1mM
PMSF
nolabel
3
Sample conditions
Ionic strength: 100mM NaCl mM / Label: conditions_1 / pH: 6.5 / Pressure: 1 atm / Temperature: 303 K
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NMR measurement
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker AVANCE II
Bruker
AVANCEII
600
1
Bruker AVANCE III
Bruker
AVANCEIII
500
3
Varian UNITYPLUS
Varian
UNITYPLUS
800
2
Varian UNITYPLUS
Varian
UNITYPLUS
900
4
Varian UNITYPLUS
Varian
UNITYPLUS
600
5
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Processing
NMR software
Name
Developer
Classification
CSRosetta
DavidBaker
structurecalculation
NMRView
Johnson, OneMoonScientific
chemicalshiftassignment
NMRPipe
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
processing
NMRView
Johnson, OneMoonScientific
peakpicking
Refinement
Method: simulated annealing / Software ordinal: 1
NMR representative
Selection criteria: medoid
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 8
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