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- PDB-1dwm: Solution structure of Linum usitatissinum trypsin inhibitor (LUTI) -

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Basic information

Entry
Database: PDB / ID: 1dwm
TitleSolution structure of Linum usitatissinum trypsin inhibitor (LUTI)
ComponentsLINUM USITATISSINUM TRYPSIN INHIBITOR
KeywordsSERINE PROTEINASE INHIBITOR / TRYPSIN INHIBITOR
Function / homology
Function and homology information


serine-type endopeptidase inhibitor activity / response to wounding
Similarity search - Function
Trypsin Inhibitor V, subunit A / Proteinase inhibitor I13, potato inhibitor I / Proteinase inhibitor I13, potato inhibitor I superfamily / Potato inhibitor I family / Potato inhibitor I family signature. / Trypsin Inhibitor V; Chain A / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Proteinase inhibitor
Similarity search - Component
Biological speciesLINUM USITATISSIMUM (flax)
MethodSOLUTION NMR / simulated annealing
AuthorsCierpicki, T. / Otlewski, J.
CitationJournal: J.Mol.Biol. / Year: 2000
Title: Determination of a High Precision Structure of a Novel Protein, Linum Usitatissimum Trypsin Inhibitor (Luti), Using Computer-Aided Assignment of Noesy Cross-Peaks
Authors: Cierpicki, T. / Otlewski, J.
History
DepositionDec 8, 1999Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 17, 1999Provider: repository / Type: Initial release
Revision 1.1May 7, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
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: LINUM USITATISSINUM TRYPSIN INHIBITOR


Theoretical massNumber of molelcules
Total (without water)7,6521
Polymers7,6521
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)20 / 40LEAST RESTRAINT VIOLATION AND LOWEST ENERGY
Representative

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Components

#1: Protein LINUM USITATISSINUM TRYPSIN INHIBITOR / LUTI


Mass: 7651.771 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) LINUM USITATISSIMUM (flax) / Organ: SEED / References: UniProt: P82381*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131DQF-COSY
1411H-15N HSQC
NMR detailsText: THE STRUCTURE WAS DETERMINED BASING ON 1760 EXPERIMENTAL RESTRAINTS DERIVED FROM TWO DIMENSIONAL 1H NMR EXPERIMENTS. NOESY CROSSPEAKS WERE ASSIGNED AUTOMATICALY USING NOAH/DYANA PROGRAM. ...Text: THE STRUCTURE WAS DETERMINED BASING ON 1760 EXPERIMENTAL RESTRAINTS DERIVED FROM TWO DIMENSIONAL 1H NMR EXPERIMENTS. NOESY CROSSPEAKS WERE ASSIGNED AUTOMATICALY USING NOAH/DYANA PROGRAM. STRUCTURE REFINEMENT WAS ACCOMPLISHED IN CNS.

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Sample preparation

DetailsContents: 10% H2O/90% D2O
Sample conditionspH: 4.3 / Temperature: 293 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CNS0.9BRUNGERrefinement
NMRPIPEstructure solution
SPARKYstructure solution
DYANAstructure solution
CNSstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION AND LOWEST ENERGY
Conformers calculated total number: 40 / Conformers submitted total number: 20

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