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- PDB-2mlp: MICROCIN LEADER PEPTIDE FROM E. COLI, NMR, 25 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 2mlp
TitleMICROCIN LEADER PEPTIDE FROM E. COLI, NMR, 25 STRUCTURES
ComponentsMCBA PROPEPTIDE
KeywordsLEADER PEPTIDE / PROPEPTIDE / ANTIBIOTIC
Function / homologynegative regulation of DNA replication / killing of cells of another organism / defense response to bacterium / Bacteriocin microcin B17
Function and homology information
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / distance geometry
AuthorsKim, S. / Sinha Roy, R. / Walsh, C.T. / Baleja, J.D.
CitationJournal: Chem.Biol. / Year: 1998
Title: Role of the microcin B17 propeptide in substrate recognition: solution structure and mutational analysis of McbA1-26.
Authors: Roy, R.S. / Kim, S. / Baleja, J.D. / Walsh, C.T.
History
DepositionJan 21, 1998Processing site: BNL
Revision 1.0Jul 22, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 12, 2012Group: Other
Revision 1.4Mar 13, 2013Group: Other
Revision 1.5Mar 16, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MCBA PROPEPTIDE


Theoretical massNumber of molelcules
Total (without water)2,7761
Polymers2,7761
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)25 / 30RANDOM
Representative

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Components

#1: Protein/peptide MCBA PROPEPTIDE


Mass: 2776.257 Da / Num. of mol.: 1 / Fragment: LEADER PEPTIDE
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: ZK4 / Plasmid: PPY113 / Production host: Escherichia coli (E. coli) / References: UniProt: P05834

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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: 5.7 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX 500 / Manufacturer: Bruker / Model: AMX 500 / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
DGIIHAVELrefinement
Insight IIIIstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION. MULTIPLE STRUCTURES WERE CALCULATED FROM NMR DATA. PAIRWISE R.M.S.D. CALCULATED FOR RESIDUES 5 - 21 BACKBONE ATOMS : 0.4 A ALL HEAVY ATOMS: 1.0 A
NMR ensembleConformer selection criteria: RANDOM / Conformers calculated total number: 30 / Conformers submitted total number: 25

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