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- PDB-1zfo: AMINO-TERMINAL LIM-DOMAIN PEPTIDE OF LASP-1, NMR -

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Basic information

Entry
Database: PDB / ID: 1zfo
TitleAMINO-TERMINAL LIM-DOMAIN PEPTIDE OF LASP-1, NMR
ComponentsLASP-1
KeywordsMETAL BINDING PROTEIN / LIM DOMAIN / ZINC-FINGER / METAL-BINDING PROTEIN
Function / homology
Function and homology information


monoatomic ion transmembrane transporter activity / cortical actin cytoskeleton / monoatomic ion transport / actin binding / metal ion binding
Similarity search - Function
: / LIM domain / Zinc finger, LIM-type / LIM domain profile.
Similarity search - Domain/homology
LIM and SH3 domain protein 1
Similarity search - Component
Biological speciesSus scrofa (pig)
MethodSOLUTION NMR
AuthorsHammarstrom, A. / Berndt, K.D. / Sillard, R. / Adermann, K. / Otting, G.
CitationJournal: Biochemistry / Year: 1996
Title: Solution structure of a naturally-occurring zinc-peptide complex demonstrates that the N-terminal zinc-binding module of the Lasp-1 LIM domain is an independent folding unit.
Authors: Hammarstrom, A. / Berndt, K.D. / Sillard, R. / Adermann, K. / Otting, G.
History
DepositionMay 6, 1996Processing site: BNL
Revision 1.0Nov 8, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations ...Database references / Derived calculations / Other / Structure summary
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_keywords / 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 / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_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_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_keywords.text / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Nov 20, 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: LASP-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)3,6152
Polymers3,5491
Non-polymers651
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein/peptide LASP-1


Mass: 3549.239 Da / Num. of mol.: 1 / Fragment: ZF-1 AMINO-TERMINAL LIM-DOMAIN PEPTIDE
Source method: isolated from a genetically manipulated source
Details: IDENTICAL TO 30 N-TERMINAL RESIDUES OF HUMAN LASP-1
Source: (gene. exp.) Sus scrofa (pig) / Organ: INTESTINE / References: UniProt: P80171
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 5.5 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR softwareName: OPAL / Developer: LUGINBUHL,GUNTERT,BILLETER,WUTHRICH / Classification: refinement
NMR ensembleConformers submitted total number: 20

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