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- PDB-2leu: HIGH RESOLUTION 1H NMR STUDY OF LEUCOCIN A IN 90% AQUEOUS TRIFLUO... -

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Basic information

Entry
Database: PDB / ID: 2leu
TitleHIGH RESOLUTION 1H NMR STUDY OF LEUCOCIN A IN 90% AQUEOUS TRIFLUOROETHANOL (TFE) (0.1% TFA), 18 STRUCTURES
ComponentsLEUCOCIN A
KeywordsANTIBACTERIAL PEPTIDE / BACTERIOCIN
Function / homologyBacteriocin, class IIa / Bacteriocin, class IIa, conserved site / Bacteriocin class IIa domain superfamily / Class II bacteriocin / Bacteriocin class IIa family signature. / killing of cells of another organism / defense response to bacterium / extracellular region / Bacteriocin leucocin-A
Function and homology information
Biological speciesLeuconostoc gelidum (bacteria)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING
AuthorsGallagher, N.L.F. / Sailer, M. / Niemczura, W.P. / Nakashima, T.T. / Stiles, M.E. / Vederas, J.C.
Citation
Journal: Biochemistry / Year: 1997
Title: Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria.
Authors: Fregeau Gallagher, N.L. / Sailer, M. / Niemczura, W.P. / Nakashima, T.T. / Stiles, M.E. / Vederas, J.C.
#1: Journal: Appl.Environ.Microbiol. / Year: 1995
Title: Molecular Characterization of Genes Involved in the Production of the Bacteriocin Leucocin a from Leuconostoc Gelidum
Authors: Van Belkum, M.J. / Stiles, M.E.
#2: Journal: Biochemistry / Year: 1993
Title: 15N-and 13C-Labeled Media from Anabaena Sp. For Universal Isotopic Labeling of Bacteriocins: NMR Resonance Assignments of Leucocin a from Leuconostoc Gelidum and Nisin a from Lactococcus Lactis
Authors: Sailer, M. / Helms, G.L. / Henkel, T. / Niemczura, W.P. / Stiles, M.E. / Vederas, J.C.
#3: Journal: J.Am.Chem.Soc. / Year: 1992
Title: NMR Assignment of Leucocin A, a Bacteriocin from Leuconostoc Gelidum, Supported by a Stable Isotope Labeling Technique for Peptides and Proteins
Authors: Henkel, T. / Sailer, M. / Helms, G.L. / Stiles, M.E. / Vederas, J.C.
#4: Journal: J.Bacteriol. / Year: 1991
Title: Characterization of Leucocin A-Ual 187 and Cloning of the Bacteriocin Gene from Leuconostoc Gelidum
Authors: Hastings, J.W. / Sailer, M. / Johnson, K. / Roy, K.L. / Vederas, J.C. / Stiles, M.E.
History
DepositionMay 20, 1997Processing site: BNL
Revision 1.0Nov 26, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4Nov 6, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: LEUCOCIN A


Theoretical massNumber of molelcules
Total (without water)3,9371
Polymers3,9371
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)18 / 20LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein/peptide LEUCOCIN A


Mass: 3937.323 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Leuconostoc gelidum (bacteria) / Strain: UAL 187 / References: UniProt: P34034
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131DQF-COSY

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Sample preparation

Sample conditionspH: 2.8 / Temperature: 299 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITY 500 / Manufacturer: Varian / Model: UNITY 500 / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
DGIIHAVELrefinement
DGII (MSI)(MSI)structure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 20 / Conformers submitted total number: 18

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