- PDB-1y9j: Solution structure of the rat Sly1 N-terminal domain -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 1y9j
Title
Solution structure of the rat Sly1 N-terminal domain
Components
Sec1 family domain containing protein 1
Keywords
PROTEIN TRANSPORT / membrane traffic / Sly1 / SM proteins / SNAREs / protein NMR
Function / homology
Function and homology information
: / regulation of protein transport / post-Golgi vesicle-mediated transport / regulation of ER to Golgi vesicle-mediated transport / COPII-mediated vesicle transport / : / negative regulation of autophagosome assembly / cis-Golgi network / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / syntaxin binding ...: / regulation of protein transport / post-Golgi vesicle-mediated transport / regulation of ER to Golgi vesicle-mediated transport / COPII-mediated vesicle transport / : / negative regulation of autophagosome assembly / cis-Golgi network / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / syntaxin binding / Golgi-associated vesicle / Golgi cisterna membrane / endoplasmic reticulum to Golgi vesicle-mediated transport / vesicle-mediated transport / intracellular protein transport / cell morphogenesis / response to toxic substance / response to hypoxia / Golgi membrane / endoplasmic reticulum membrane / protein-containing complex binding / plasma membrane / cytosol Similarity search - Function
Sec1familydomaincontainingprotein1 / Syntaxin binding protein 1- like 2 / Vesicle transport-related protein Ra410 / Sly1p
Mass: 17678.289 Da / Num. of mol.: 1 / Fragment: N-terminal domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Scfd1, Ra410, Sly1, Stxbp1l2 / Plasmid: PGEX-KG / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 competent cells / References: UniProt: Q62991
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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
1
2
1
3D 15N-separated NOESY
1
3
1
3D 13C-separated NOESY
NMR details
Text: This structure was determined using standard triple resonance techniques
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
1.2 mM Sly1 N-terminal domain U-15N, 20 mM MES(pH 5.7), 200 mM KCl, 1 mM DTT
20mMMES(pH5.7), 200mMKCl, 1mMDTT
2
1.2 mM Sly1 N-terminal domain U-15N,13C, 20 mM MES(pH 5.7), 200 mM KCl, 1 mM DTT
20mMMES(pH5.7), 200mMKCl, 1mMDTT
3
1 mM Sly1 N-terminal domain U-10%13C, 20 mM MES(pH 5.7), 200 mM KCl, 1 mM DTT
20mMMES(pH5.7), 200mMKCl, 1mMDTT
Sample conditions
Ionic strength: 200 mM KCl / pH: 5.7 / Pressure: ambient / Temperature: 300 K
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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
600
1
Varian INOVA
Varian
INOVA
500
2
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Processing
NMR software
Name
Version
Developer
Classification
VNMR
6.1C
Varian
collection
NMRPipe
2.3
Delaglio
processing
NMRView
4.1.2
Johnson
dataanalysis
TALOS
2003.027.13.05
Delaglio
dataanalysis
CNS
0.9
Brunger
refinement
Refinement
Method: torsion angle dynamics / Software ordinal: 1 Details: A total of 2493 restraints were used for the final calculations, including 2133 NOEs (of which 738 were long-range NOEs), 132 hydrogen bond restraints and 228 torsion angle restraints.
NMR representative
Selection criteria: lowest energy
NMR ensemble
Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 1400 / Conformers submitted total number: 20
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