Evidence: equilibrium centrifugation, sedimentation equilibrium by analytical ultracentrifugation supports the kinetic model observed by NMR
Type
Name
Symmetry operation
Number
identity operation
1_555
1
NMR ensembles
Data
Criteria
Number of conformers (submitted / calculated)
10 / 1100
structures with the lowest energy
Representative
Model #1
best fits pre data
-
Components
#1: Protein/peptide
Huntingtin / / Huntington disease protein / HD protein
Mass: 2743.116 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HTT, HD, IT15 / Production host: Escherichia coli (E. coli) / References: UniProt: P42858
-
Experimental details
-
Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Sample state
Spectrometer-ID
Type
1
1
2
isotropic
1
2D 1H-15N HSQC
1
2
2
isotropic
1
2D 1H-13C CT HSQC
2
3
2
isotropic
1
3DCBCA(CO)NH
2
4
2
isotropic
1
3D HN(CA)CB
2
5
4
isotropic
2
3D TOCSY-HSQC
1
6
3
isotropic
1
13CA SQ CPMG
1
7
5
isotropic
3
13CA SQ CPMG
1
8
3
isotropic
1
15N SQ CPMG
1
9
5
isotropic
3
15N SQ CPMG
2
10
4
isotropic
1
1HNPRE
1
11
6
isotropic
13CA SQ CPMG
1
12
6
isotropic
15N SQ CPMG
-
Sample preparation
Details
Type
Solution-ID
Contents
Details
Label
Solvent system
solution
2
1 mM [U-13C; U-15N] httNT-Q7, 90% H2O/10% D2O
20mMsodiumphosphate, pH6.5, 50mMsodiumchloride
U_13C_15N_sample
90% H2O/10% D2O
solution
4
0.6 mM [U-15N] httNT-Q7, 90% H2O/10% D2O
20mMsodiumphosphate, pH6.5, 50mMsodiumchloride
15N_sample
90% H2O/10% D2O
solution
3
1 mM 2-13C glucose; U-15N httNT-Q7, 90% H2O/10% D2O
20mMsodiumphosphate, pH6.5, 50mMsodiumchloride
2-13C_15N_sample
90% H2O/10% D2O
solution
5
0.75 mM 2-13C glucose; U-15N httNT-Q7, 90% H2O/10% D2O
20mMsodiumphosphate, pH6.5, 50mMsodiumchloride
2-13C_15N_sample
90% H2O/10% D2O
solution
6
0.4 mM 2-13C glucose; U-15N httNT-Q7, 90% H2O/10% D2O
20mMsodiumphosphate, pH6.5, 50mMsodiumchloride
2-13C_15N_sample
90% H2O/10% D2O
Sample
Conc. (mg/ml)
Component
Isotopic labeling
Solution-ID
1mM
httNT-Q7
[U-13C; U-15N]
2
0.6mM
httNT-Q7
[U-15N]
4
1mM
2-13C glucose, httNT-Q7
[U-15N]
3
0.75mM
2-13C glucose, httNT-Q7
[U-15N]
5
0.4mM
2-13C glucose, httNT-Q7
[U-15N]
6
Sample conditions
Conditions-ID
Details
Ionic strength
Label
pH
Pressure (kPa)
Temperature (K)
1
20mMsodiumphosphate, pH6.5, 50mMsodiumchloride
50mM
conditions_1
6.5
1atm
278K
2
20mMsodiumphosphate, pH6.5, 50mMsodiumchloride
50mM
conditions_2
6.5
1atm
283K
-
NMR measurement
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker AVANCE III
Bruker
AVANCEIII
600
1
Bruker AVANCE III
Bruker
AVANCEIII
800
2
Bruker AVANCE III
Bruker
AVANCEIII
900
3
-
Processing
NMR software
Name
Version
Developer
Classification
Xplor-NIH
2.49
C.D. Schwieters, J.J. Kuszewski, N. Tjandra, andG.M. Clore
structurecalculation
Analysis
2.4
CCPN
chemicalshiftassignment
NMRDraw
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
peakpicking
NMRPipe
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
dataanalysis
NMRPipe
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
processing
TopSpin
BrukerBiospin
collection
Refinement
Method: simulated annealing / Software ordinal: 1 Details: utilized rigid backbone coordinates for helix region and employed Xplor-NIH's strict symmetry facility to generage full tetramer from protomer coordinates.
NMR representative
Selection criteria: best fits pre data
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 1100 / Conformers submitted total number: 10
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