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- PDB-1uuc: solution structure of a chimeric LEKTI-domain -

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Basic information

Entry
Database: PDB / ID: 1uuc
Titlesolution structure of a chimeric LEKTI-domain
ComponentsSERINE PROTEASE INHIBITOR KAZAL-TYPE 5
KeywordsSERINE PROTEINASE INHIBITOR / PROTEASE / CHAMELEON SEQUENCE
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 / extracellular matrix organization / negative regulation of angiogenesis / 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 / cytosol / cytoplasm
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
AuthorsTidow, H. / Lauber, T. / Roesch, P. / Marx, U.C.
CitationJournal: Biochemistry / Year: 2004
Title: The Solution Structure of a Chimeric Lekti Domain Reveals a Chameleon Sequence
Authors: Tidow, H. / Lauber, T. / Vitzithum, K. / Sommerhoff, C. / Roesch, P. / Marx, U.C.
History
DepositionDec 18, 2003Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 24, 2004Provider: 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: Other / Category: pdbx_database_status
Item: _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr
Revision 1.4Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
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


Theoretical massNumber of molelcules
Total (without water)6,4081
Polymers6,4081
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)30 / 160LOWEST ENERGY; LEAST RESTRAINT VIOLATION
RepresentativeModel #1

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Components

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


Mass: 6407.543 Da / Num. of mol.: 1
Fragment: CHIMERIC PROTEIN OF LEKTI DOMAIN ONE, RESIDUES 23-77
Mutation: YES
Source method: isolated from a genetically manipulated source
Details: DISULFIDE BONDS BETWEEN CYS 8 AND CYS 44, BETWEEN CYS 22 AND CYS 41
Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: I.E. VAGINAL EPITHELIUM / Plasmid: PET32A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): ORIGAMI / Variant (production host): DE3 / References: UniProt: Q9NQ38
Compound detailsENGINEERED MUTATION IN CHAIN A PRO 28 FROM PHE ENGINEERED MUTATION IN CHAIN A ILE 29 FROM PHE
Sequence detailsTHE LEKTI SEQUENCE PROVIDED BY SWISSPROT DIFFERS FROM THAT GIVEN IN THE ORIGINAL PAPER BY MAEGERT ...THE LEKTI SEQUENCE PROVIDED BY SWISSPROT DIFFERS FROM THAT GIVEN IN THE ORIGINAL PAPER BY MAEGERT ET AL., 1999. IN THIS ENTRY THE SEQUENCE REFERS TO THE ORIGINAL PAPER AND IS ALSO IDENTICAL (EXCEPT FOR THE TWO MUTATIONS AT POSITIONS 28 AND 29) TO THAT OF LEKTI DOMAIN ONE (HF6478, PDB-CODE 1HDL) AS ISOLATED FROM HUMAN BLOOD FILTRATE (REFERENCES: MAGERT ET AL., 1999, J. BIOL. CHEM. 274, 21499-21502. LAUBER ET AL.,2001, PROTEIN EXPR. PURIF. 22, 108-112; LAUBER ET AL., 2003, J. MOL. BIOL., 328, 205-219.) THUS, THE SEQUENCE IN THIS ENTRY REFERS TO RESIDUES 23 TO 77 OF FULL-LENGTH LEKTI.

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D-TOCSY
1212D-COSY
1312D-NOESY
1411H
15115N-HSQC
161HNHA
1713D-1H
18115N-TOCSY-HSQC
1913D-1H
110115N-NOESY-HSQC
11113D-1H
112115N
113115N-HMQC-NOESY-HSQC
NMR detailsText: THIS STRUCTURE WAS DETERMINED USING STANDARD NMR-TECHNIQUES ON 15N-LABELED AND UNLABELED PROTEIN

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Sample preparation

Sample conditionsIonic strength: 10 mM / pH: 5.0 / Pressure: 1 atm / 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
X-PLOR3.8.5.1BRUNGERrefinement
NDEE; NMRVIEW5.1.4structure solution
RefinementMethod: simulated annealing / Software ordinal: 1 / Details: SIMULATED ANNEALING
NMR ensembleConformer selection criteria: LOWEST ENERGY; LEAST RESTRAINT VIOLATION
Conformers calculated total number: 160 / Conformers submitted total number: 30

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