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- PDB-2afe: Solution Structure of Asl1650, an Acyl Carrier Protein from Anaba... -

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Basic information

Entry
Database: PDB / ID: 2afe
TitleSolution Structure of Asl1650, an Acyl Carrier Protein from Anabaena sp. PCC 7120 with a Variant Phosphopantetheinylation-Site Sequence
Componentsprotein Asl1650
KeywordsLIGAND BINDING PROTEIN / twisted antiparallel helical bundle / acyl carrier protein family / Structural Genomics / PSI / Protein Structure Initiative / Joint Center for Structural Genomics / JCSG
Function / homology
Function and homology information


phosphopantetheine binding
Similarity search - Function
ACP-like / Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A / Polyketide synthase, phosphopantetheine-binding domain / Phosphopantetheine attachment site / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesNostoc sp. (bacteria)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsJohnson, M.A. / Peti, W. / Herrmann, T. / Wilson, I.A. / Wuthrich, K. / Joint Center for Structural Genomics (JCSG)
CitationJournal: Protein Sci. / Year: 2006
Title: Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence
Authors: Johnson, M.A. / Peti, W. / Herrmann, T. / Wilson, I.A. / Wuthrich, K.
History
DepositionJul 25, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 16, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.3Oct 20, 2021Group: Data collection / Database references
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
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: protein Asl1650


Theoretical massNumber of molelcules
Total (without water)10,0881
Polymers10,0881
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)1 / 100Representative conformer; Conformer with the lowest rmsd to the mean coordinates of the ensemble
Representative

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Components

#1: Protein protein Asl1650


Mass: 10088.395 Da / Num. of mol.: 1 / Mutation: Cys10Ala
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Nostoc sp. (bacteria) / Strain: PCC 7120 / Description: synonym Nostoc sp. PCC 7120 / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-RIL (Stratagene) / References: UniProt: Q8YWG3

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
1223D 15N-separated NOESY
1332D NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
12mM Asl1650 U-15N,13C; 20mM phosphate buffer, pH 6.0; 250 mM NaCl; 2mM NaN390% H2O/10% D2O
22mM Asl1650 U-15N; 20mM phosphate buffer, pH 6.0; 250 mM NaCl; 2mM NaN390% H2O/10% D2O
32mM Asl1650; 20mM phosphate buffer, pH 6.0; 250mM NaCl; 2mM NaN399% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
1250 mM NaCl 6ambient 303 K
2250 mM NaCl 6ambient 303 K
3250 mM NaCl 6ambient 303 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE9001
Bruker AVANCEBrukerAVANCE6002
Bruker AVANCEBrukerAVANCE5003

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Processing

NMR software
NameVersionDeveloperClassification
ATNOS1Herrmann T, Guntert P, Wuthrich Kstructure solution
CANDID1Herrmann T, Guntert P, Wuthrich Kstructure solution
DYANA6.01Guntert P, Mumenthaler C, Wuthrich Kstructure solution
OPALp1Luginbuhl P, Guntert P, Billeter M, Wuthrich Krefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
Details: automated NOESY peak picking, automated NOE assignment
NMR ensembleConformer selection criteria: Representative conformer; Conformer with the lowest rmsd to the mean coordinates of the ensemble
Conformers calculated total number: 100 / Conformers submitted total number: 1

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