SYNDECAN-4 / AMPHIGLYCAN / RYUDOCAN CORE PROTEIN / SYND4
Mass: 3314.850 Da / Num. of mol.: 2 / Fragment: WHOLE CYTOPLASMIC DOMAIN (RESIDUES 171-198) / Source method: obtained synthetically Details: This peptide was chemically synthesized. The sequence of this petide occurs naturally in humans (Homo Sapiens). References: UniProt: P31431
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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 NOESY
2
2
2
DQF-COSY
3
3
3
2D NOESY
NMR details
Text: This structure was determined using standard 2D homonuclear techniques.
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
2-4mM Syndecan-4 cytoplasmic domain;Molar ratio of 4:1(syndecan-4 peptide:PIP2);50mM sodium phosphate;90% H2O 10% D2O
90% H2O/10% D2O
2
2-4mM Syndecan-4 cytoplasmic domain;Molar ratio of 4:1(syndecan-4 peptide:PIP2);50mM sodium phosphate;90% H2O 10% D2O
90% H2O/10% D2O
3
2-4mM Syndecan-4 cytoplasmic domain;Molar ratio of 4:1(syndecan-4 peptide:PIP2);50mM sodium phosphate;90% H2O 10% D2O
100% D2O
Sample conditions
Conditions-ID
Ionic strength
pH
Pressure (kPa)
Temperature (K)
1
50mMsodiumphosphate
7.4
1atm
298K
2
50mMsodiumphosphate
7.4
1atm
298K
3
50mMsodiumphosphate
7.4
1atm
298K
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NMR measurement
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker DRX
Bruker
DRX
500
1
Bruker DRX
Bruker
DRX
500
2
Bruker DRX
Bruker
DRX
500
3
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Processing
NMR software
Name
Version
Developer
Classification
XwinNMR
2.5
Bruker
collection
XwinNMR
2.5
Bruker
processing
Sparky
3.6
James, T.
dataanalysis
X-PLOR
3.851
Brunger, A.T
refinement
Refinement
Method: simulated annealing / Software ordinal: 1
NMR representative
Selection criteria: minimized average structure
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 90 / Conformers submitted total number: 15
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