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- PDB-1x62: Solution structure of the LIM domain of carboxyl terminal LIM dom... -

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Basic information

Entry
Database: PDB / ID: 1x62
TitleSolution structure of the LIM domain of carboxyl terminal LIM domain protein 1
ComponentsC-terminal LIM domain protein 1
KeywordsSTRUCTURAL PROTEIN / LIM domain / PDZ and LIM domain protein 1 / LIM domain protein CLP-36 / C-terminal LIM domain protein 1 / contractile protein / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI
Function / homology
Function and homology information


establishment or maintenance of actin cytoskeleton polarity / muscle structure development / muscle alpha-actinin binding / maintenance of cell polarity / cadherin binding involved in cell-cell adhesion / fibroblast migration / stress fiber assembly / filamentous actin / stress fiber / adherens junction ...establishment or maintenance of actin cytoskeleton polarity / muscle structure development / muscle alpha-actinin binding / maintenance of cell polarity / cadherin binding involved in cell-cell adhesion / fibroblast migration / stress fiber assembly / filamentous actin / stress fiber / adherens junction / Z disc / heart development / actin binding / actin cytoskeleton organization / transcription regulator complex / response to oxidative stress / transcription coactivator activity / cytoskeleton / response to hypoxia / focal adhesion / regulation of transcription by RNA polymerase II / metal ion binding / cytoplasm
Similarity search - Function
PDZ and LIM domain protein 1 / Zasp-like motif / ZASP-like motif / Domain of unknown function DUF4749 / Domain of unknown function (DUF4749) / : / Cysteine Rich Protein / Cysteine Rich Protein / LIM zinc-binding domain signature. / LIM domain ...PDZ and LIM domain protein 1 / Zasp-like motif / ZASP-like motif / Domain of unknown function DUF4749 / Domain of unknown function (DUF4749) / : / Cysteine Rich Protein / Cysteine Rich Protein / LIM zinc-binding domain signature. / LIM domain / Zinc-binding domain present in Lin-11, Isl-1, Mec-3. / Zinc finger, LIM-type / LIM domain profile. / PDZ domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Ribbon / Mainly Beta
Similarity search - Domain/homology
PDZ and LIM domain protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsQin, X.R. / Nagashima, T. / Hayashi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: To be published
Title: Solution structure of the LIM domain of carboxyl terminal LIM domain protein 1
Authors: Qin, X.R. / Nagashima, T. / Hayashi, F. / Yokoyama, S.
History
DepositionMay 17, 2005Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 17, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: C-terminal LIM domain protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)8,7053
Polymers8,5741
Non-polymers1312
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 / 100target function, structures with the lowest energy, structures with the least restraint violations
RepresentativeModel #1lowest energy

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Components

#1: Protein C-terminal LIM domain protein 1 / LIM domain protein CLP-36 / Elfin


Mass: 8573.706 Da / Num. of mol.: 1 / Fragment: LIM domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Description: cell free protein synthesis / Gene: PDLIM1, CLIM1, CLP36 / Plasmid: P040830-06 / References: UniProt: O00151
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1213D 13C-separated NOESY
NMR detailsText: spectrometer_id 1 for 3D_15N_separated_NOESY; spectrometer_id 2 for 3D_13C_separated_NOESY

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Sample preparation

DetailsContents: 1.18mM 13C,15N-labeled protein; 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3, 0.01mM ZnCl2
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA8001
Varian INOVAVarianINOVA9002

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Processing

NMR software
NameVersionDeveloperClassification
VNMR6.1CVariancollection
NMRPipe20031121Delaglio,F.processing
NMRView5.0.4Johnson,B.A.data analysis
KUJIRA0.9296Kobayashi,N.data analysis
CYANA2.0.17Guntert,P.structure solution
CYANA2.0.17Guntert,P.refinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function, structures with the lowest energy, structures with the least restraint violations
Conformers calculated total number: 100 / Conformers submitted total number: 20

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