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- PDB-2cti: DETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE ... -

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Entry
Database: PDB / ID: 2cti
TitleDETERMINATION OF THE COMPLETE THREE-DIMENSIONAL STRUCTURE OF THE TRYPSIN INHIBITOR FROM SQUASH SEEDS IN AQUEOUS SOLUTION BY NUCLEAR MAGNETIC RESONANCE AND A COMBINATION OF DISTANCE GEOMETRY AND DYNAMICAL SIMULATED ANNEALING
ComponentsTRYPSIN INHIBITOR
KeywordsPROTEINASE INHIBITOR (TRYPSIN)
Function / homologyProteinase inhibitor I7, squash / Squash family serine protease inhibitor / Squash family of serine protease inhibitors signature. / Plant trypsin inhibitors / Proteinase/amylase inhibitor domain superfamily / serine-type endopeptidase inhibitor activity / extracellular region / Trypsin inhibitor 1
Function and homology information
Biological speciesCucurbita maxima (winter squash)
MethodSOLUTION NMR
AuthorsHolak, T.A. / Gondol, D. / Otlewski, J. / Wilusz, T.
Citation
Journal: J.Mol.Biol. / Year: 1989
Title: Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry ...Title: Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing.
Authors: Holak, T.A. / Gondol, D. / Otlewski, J. / Wilusz, T.
#1: Journal: J.Mol.Biol. / Year: 1989
Title: Nuclear Magnetic Resonance Solution and X-Ray Structures of Squash Trypsin Inhibitor Exhibit the Same Conformation of the Proteinase Binding Loop
Authors: Holak, T.A. / Bode, W. / Huber, R. / Otlewski, J. / Wilusz, T.
History
DepositionAug 28, 1990Processing site: BNL
Revision 1.0Jan 15, 1992Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Oct 30, 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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Assembly

Deposited unit
A: TRYPSIN INHIBITOR


Theoretical massNumber of molelcules
Total (without water)3,2801
Polymers3,2801
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)5 / -
Representative

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Components

#1: Protein/peptide TRYPSIN INHIBITOR


Mass: 3279.919 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Cucurbita maxima (winter squash) / References: UniProt: P01074
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

SoftwareName: SQUASH / Classification: phasing
NMR software
NameDeveloperClassification
DISGEOHAVEL,WUTHRICHrefinement
X-PLORBRUNGERrefinement
NMR ensembleConformers submitted total number: 5

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