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- PDB-2l7t: Solution structure of the MFS-bound Sans CEN2 peptide -

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Basic information

Entry
Database: PDB / ID: 2l7t
TitleSolution structure of the MFS-bound Sans CEN2 peptide
ComponentsMFS-bound Sans CEN2 peptide
KeywordsUNKNOWN FUNCTION / PROTEIN Peptide
Function / homology
Function and homology information


photoreceptor cell cilium / regulation of clathrin-dependent endocytosis / equilibrioception / sensory perception of light stimulus / photoreceptor connecting cilium / inner ear receptor cell stereocilium organization / photoreceptor cell maintenance / Sensory processing of sound by outer hair cells of the cochlea / Sensory processing of sound by inner hair cells of the cochlea / ciliary base ...photoreceptor cell cilium / regulation of clathrin-dependent endocytosis / equilibrioception / sensory perception of light stimulus / photoreceptor connecting cilium / inner ear receptor cell stereocilium organization / photoreceptor cell maintenance / Sensory processing of sound by outer hair cells of the cochlea / Sensory processing of sound by inner hair cells of the cochlea / ciliary base / inner ear morphogenesis / spectrin binding / Cajal body / photoreceptor inner segment / ciliary basal body / sensory perception of sound / actin cytoskeleton / nuclear speck / centrosome / identical protein binding / plasma membrane / cytosol
Similarity search - Function
USH1G, SAM domain / SAM domain (Sterile alpha motif) / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily
Similarity search - Domain/homology
pre-mRNA splicing regulator USH1G
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsPan, L. / Wu, L. / Wei, Z. / Zhang, M.
CitationJournal: Science / Year: 2011
Title: Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo.
Authors: Wu, L. / Pan, L. / Wei, Z. / Zhang, M.
History
DepositionDec 22, 2010Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Mar 2, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MFS-bound Sans CEN2 peptide


Theoretical massNumber of molelcules
Total (without water)1,3151
Polymers1,3151
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 200structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide MFS-bound Sans CEN2 peptide / 11-mer peptide from Usher syndrome type-1G protein / Sans


Mass: 1315.382 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: The peptide was chemically synthesized. / Source: (synth.) Homo sapiens (human) / References: UniProt: Q495M9

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: 2D 1H-1H NOESY

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Sample preparation

DetailsContents: 50 mM sodium chloride-1, 1 mM DTT-2, 1 mM EDTA-3, 50 mM potassium phosphate-4, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentSolution-ID
50 mMsodium chloride-11
1 mMDTT-21
1 mMEDTA-31
50 mMpotassium phosphate-41
Sample conditionsIonic strength: 0.1 / pH: 6.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA5001
Varian INOVAVarianINOVA7502

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Processing

NMR software
NameDeveloperClassification
PIPPGarrettchemical shift assignment
PIPPGarrettpeak picking
CNSrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 10 / Representative conformer: 10

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