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- PDB-1h0z: LEKTI domain six -

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Basic information

Entry
Database: PDB / ID: 1h0z
TitleLEKTI domain six
ComponentsSERINE PROTEASE INHIBITOR KAZAL-TYPE 5, CONTAINS HEMOFILTRATE PEPTIDE HF6478, HEMOFILTRATE PEPTIDE HF7665
KeywordsSERINE PROTEINASE INHIBITOR
Function / homology
Function and homology information


negative regulation of antibacterial peptide production / epidermal lamellar body / regulation of timing of anagen / epidermal cell differentiation / hair cell differentiation / Formation of the cornified envelope / negative regulation of immune response / regulation of T cell differentiation / regulation of cell adhesion / epithelial cell differentiation ...negative regulation of antibacterial peptide production / epidermal lamellar body / regulation of timing of anagen / epidermal cell differentiation / hair cell differentiation / Formation of the cornified envelope / negative regulation of immune response / regulation of T cell differentiation / regulation of cell adhesion / epithelial cell differentiation / negative regulation of angiogenesis / extracellular matrix organization / central nervous system development / negative regulation of proteolysis / serine-type endopeptidase inhibitor activity / cell cortex / cell differentiation / intracellular membrane-bounded organelle / endoplasmic reticulum membrane / perinuclear region of cytoplasm / endoplasmic reticulum / extracellular region / cytoplasm / cytosol
Similarity search - Function
Kazal serine protease inhibitors family signature. / Kazal-type serine protease inhibitor domain / Wheat Germ Agglutinin (Isolectin 2); domain 1 - #30 / Kazal type serine protease inhibitors / Kazal domain superfamily / Kazal domain / Kazal domain profile. / Wheat Germ Agglutinin (Isolectin 2); domain 1 / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Serine protease inhibitor Kazal-type 5
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / simulated annealing
AuthorsLauber, T. / Roesch, P. / Marx, U.C.
CitationJournal: J.Mol.Biol. / Year: 2003
Title: Homologous Proteins with Different Folds: The Three-Dimensional Structures of Domains 1 and 6 of the Multiple Kazal-Type Inhibitor Lekti
Authors: Lauber, T. / Schulz, A. / Schweimer, K. / Adermann, K. / Marx, U.C.
History
DepositionJul 1, 2002Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 26, 2003Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 15, 2020Group: Data collection / Other / Category: pdbx_database_status / pdbx_nmr_software
Item: _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name
Revision 1.4Jun 14, 2023Group: Database references / Derived calculations / Other / Category: database_2 / pdbx_database_status / struct_sheet
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _struct_sheet.number_strands
Remark 650 HELIX DETERMINATION METHOD: AUTHOR PROVIDED.
Remark 700 SHEET DETERMINATION METHOD: AUTHOR PROVIDED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: SERINE PROTEASE INHIBITOR KAZAL-TYPE 5, CONTAINS HEMOFILTRATE PEPTIDE HF6478, HEMOFILTRATE PEPTIDE HF7665


Theoretical massNumber of molelcules
Total (without water)7,6831
Polymers7,6831
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)21 / 60LEAST ENERGY AND LEAST RESTRAINT VIOLATION
RepresentativeModel #1

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Components

#1: Protein SERINE PROTEASE INHIBITOR KAZAL-TYPE 5, CONTAINS HEMOFILTRATE PEPTIDE HF6478, HEMOFILTRATE PEPTIDE HF7665 / HF7665 / LYMPHO-EPITHELIAL KAZAL-TYPE RELATED INHIBITOR / LEKTI


Mass: 7682.533 Da / Num. of mol.: 1 / Fragment: LEKTI DOMAIN SIX (HF7665), RESIDUES 356-423 / Source method: isolated from a natural source
Details: DISULFIDE LINKAGE BETWEEN CYS A12 AND CYS A48, AND BETWEEN CYS A26 AND CYS A45
Source: (natural) HOMO SAPIENS (human) / Cell: LYMPHO EPITHELIAL CELLS / Organ: BLOOD / References: UniProt: Q9NQ38
Sequence detailsTHE SEQUENCE OF THE PROTEIN USED IN THE NMR STUDY DIFFERS FROM THAT OF THE MATCHING SWISS-PROT ...THE SEQUENCE OF THE PROTEIN USED IN THE NMR STUDY DIFFERS FROM THAT OF THE MATCHING SWISS-PROT ENTRY AT POSITION 420. RESIDUE 420 IS A GLU, NOT LYS AS IN THE SWISS-PROT ENTRY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121DQF-COSY
131CLEAN-TOCSY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING STANDARD 2D NMR EXPERIMENTS ON A NATIVE PROTEIN SAMPLE ISOLATED FROM HUMAN BLOOD FILTRATE

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Sample preparation

Sample conditionspH: 4.0 / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
3.851BRUNGERrefinement
X-PLOR3.851structure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST ENERGY AND LEAST RESTRAINT VIOLATION
Conformers calculated total number: 60 / Conformers submitted total number: 21

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