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- PDB-1pak: NMR SOLUTION STRUCTURE AND FLEXIBILITY OF A PEPTIDE ANTIGEN REPRE... -

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Basic information

Entry
Database: PDB / ID: 1pak
TitleNMR SOLUTION STRUCTURE AND FLEXIBILITY OF A PEPTIDE ANTIGEN REPRESENTING THE RECEPTOR BINDING DOMAIN OF PSEUDOMONAS AERUGINOSA
ComponentsFIMBRIAL PROTEIN PRECURSOR
KeywordsFIMBRIAL PROTEIN
Function / homology
Function and homology information


type IV pilus / type IV pilus-dependent motility / cell adhesion / membrane
Similarity search - Function
Fimbrial protein pilin / Pilin (bacterial filament) / : / Prokaryotic N-terminal methylation site. / Prokaryotic N-terminal methylation motif / Prokaryotic N-terminal methylation site / Pilin-like
Similarity search - Domain/homology
Biological speciesPseudomonas aeruginosa (bacteria)
MethodSOLUTION NMR
AuthorsMcinnes, C. / Sonnichsen, F.D. / Kay, C.M. / Hodges, R.S. / Sykes, B.D.
Citation
Journal: Biochemistry / Year: 1993
Title: NMR solution structure and flexibility of a peptide antigen representing the receptor binding domain of Pseudomonas aeruginosa.
Authors: McInnes, C. / Sonnichsen, F.D. / Kay, C.M. / Hodges, R.S. / Sykes, B.D.
#1: Journal: To be Published
Title: Conformational Differences between the Cis and Trans Proline Isomers of a Peptide Antigen Representing the Receptor Binding Domain of Pseudomonas Aeruginosa
Authors: Mcinnes, C. / Kay, C.M. / Hodges, R.S. / Sykes, B.D.
History
DepositionAug 25, 1993Processing site: BNL
Revision 1.0Jan 31, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf
Item: _pdbx_database_status.process_site
Revision 2.0Sep 25, 2024Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / chem_comp_atom / chem_comp_bond / database_2 / entity / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_rmsd_bond / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.group_PDB / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.label_seq_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_assembly_gen.asym_id_list
Revision 2.1Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: FIMBRIAL PROTEIN PRECURSOR


Theoretical massNumber of molelcules
Total (without water)1,9431
Polymers1,9431
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein/peptide FIMBRIAL PROTEIN PRECURSOR


Mass: 1943.182 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / References: UniProt: P02973
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR ensembleConformers submitted total number: 1

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