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- PDB-1fme: SOLUTION STRUCTURE OF FSD-EY, A NOVEL PEPTIDE ASSUMING A BETA-BET... -

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Entry
Database: PDB / ID: 1fme
TitleSOLUTION STRUCTURE OF FSD-EY, A NOVEL PEPTIDE ASSUMING A BETA-BETA-ALPHA FOLD
ComponentsFSD-EY PEPTIDE
KeywordsDE NOVO PROTEIN / beta-beta-alpha / zinc finger / FSD-1 / designed protein
MethodSOLUTION NMR / X-PLOR: distance geometry, refinement
AuthorsSarisky, C.A. / Mayo, S.L.
CitationJournal: J.Mol.Biol. / Year: 2001
Title: The beta-beta-alpha fold: explorations in sequence space.
Authors: Sarisky, C.A. / Mayo, S.L.
History
DepositionAug 16, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 21, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: FSD-EY PEPTIDE


Theoretical massNumber of molelcules
Total (without water)3,5481
Polymers3,5481
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)34 / 49structures with the least restraint violations
Representative

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Components

#1: Protein/peptide FSD-EY PEPTIDE


Mass: 3548.038 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: Point mutant of sequence generated by ORBIT design process

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
121DQF-COSY
131TOCSY
1422D NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
12 mM peptide90% H2O, 10% D2O, 50mM phosphate buffer, pH 5.0
22 mM peptideD2O, 50mM phosphate buffer, pH 5.0
Sample conditionspH: 5 / Pressure: ambient / Temperature: 280 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
ANSIGPer Kraulisdata analysis
VNMR6.1collection
X-PLOR3.857refinement
RefinementMethod: X-PLOR: distance geometry, refinement / Software ordinal: 1
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 49 / Conformers submitted total number: 34

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