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- PDB-1mmc: 1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2 -

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Basic information

Entry
Database: PDB / ID: 1mmc
Title1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2
ComponentsANTIMICROBIAL PEPTIDE 2
KeywordsCHITIN-BINDING / ANTIFUNGAL ANTIMICROBIAL
Function / homology
Function and homology information


chitin binding / defense response to fungus / killing of cells of another organism / defense response to bacterium
Similarity search - Function
Antimicrobial peptide, C6 type, conserved site / Plant C6 type antimicrobial peptide (AMP) signature. / Chitin-binding, type 1, conserved site / Chitin recognition protein / Chitin recognition or binding domain signature. / Chitin binding domain / Chitin-binding, type 1 / Endochitinase-like superfamily
Similarity search - Domain/homology
Antimicrobial peptide 2
Similarity search - Component
Biological speciesAmaranthus caudatus (amaranth)
MethodSOLUTION NMR
AuthorsMartins, J.C. / Maes, D. / Loris, R. / Pepermans, H.A.M. / Wyns, L. / Willem, R. / Verheyden, P.
Citation
Journal: J.Mol.Biol. / Year: 1996
Title: H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.
Authors: Martins, J.C. / Maes, D. / Loris, R. / Pepermans, H.A. / Wyns, L. / Willem, R. / Verheyden, P.
#1: Journal: FEBS Lett. / Year: 1995
Title: 1H NMR Study of the Interaction of N,N',N''-Triacetyl Chitotriose with Ac-AMP2, a Sugar Binding Antimicrobial Protein Isolated from Amaranthus Caudatus
Authors: Verheyden, P. / Pletinckx, J. / Maes, D. / Pepermans, H.A.M. / Wyns, L. / Willem, R. / Martins, J.C.
#2: Journal: Biochemistry / Year: 1992
Title: Antimicrobial Peptides from Amaranthus Caudatus Seeds with Sequence Homology to the Cysteine(Slash)Glycine Rich Domain of Chitin-Binding Proteins
Authors: Broekaert, W.F. / Marien, W. / Terras, F.R.G. / De Bolle, M.F.C. / Proost, P. / Van Damme, J. / Dillen, L. / Claeys, M. / Rees, S.B. / Vanderleyden, J. / Cammue, B.P.A.
History
DepositionOct 25, 1995Processing site: BNL
Revision 1.0Mar 8, 1996Provider: 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 / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Nov 20, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_nmr_software
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ANTIMICROBIAL PEPTIDE 2


Theoretical massNumber of molelcules
Total (without water)3,1951
Polymers3,1951
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)26 / -
Representative

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Components

#1: Protein/peptide ANTIMICROBIAL PEPTIDE 2 / AC-AMP2


Mass: 3194.782 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Amaranthus caudatus (amaranth) / Tissue: SEED / References: UniProt: P27275
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

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Processing

NMR software
NameDeveloperClassification
DIANAGUNTERT,BRAUN,WUTHRICHrefinement
AmberSINGH,WEINER,KOLLMANrefinement
NMR ensembleConformers submitted total number: 26

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