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- PDB-3ci2: REFINEMENT OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF BARLEY ... -

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Entry
Database: PDB / ID: 3ci2
TitleREFINEMENT OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF BARLEY SERINE PROTEINASE INHIBITOR 2 AND COMPARISON WITH THE STRUCTURES IN CRYSTALS
ComponentsCHYMOTRYPSIN INHIBITOR 2
KeywordsSERINE PROTEASE 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
Subtilisin-chymotrypsin inhibitor-2A
Similarity search - Component
Biological speciesHordeum vulgare (barley)
MethodSOLUTION NMR
AuthorsPoulsen, F.M.
Citation
Journal: J.Mol.Biol. / Year: 1991
Title: Refinement of the three-dimensional solution structure of barley serine proteinase inhibitor 2 and comparison with the structures in crystals.
Authors: Ludvigsen, S. / Shen, H.Y. / Kjaer, M. / Madsen, J.C. / Poulsen, F.M.
#1: Journal: J.Mol.Biol. / Year: 1991
Title: Accurate Measurements of Coupling Constants from Two-Dimensional Nuclear Magnetic Resonance Spectra of Proteins and Determination of Phi-Angles
Authors: Ludvigsen, S. / Andersen, K.V. / Poulsen, F.M.
#2: Journal: J.Magn.Reson. / Year: 1990
Title: Application of Symmetry Projection Operators to Measurements of Coupling Constants in 2D NMR Spectra of Proteins
Authors: Shen, H. / Ludvigsen, S. / Poulsen, F.M.
#3: Journal: Alfred Benzon Symp. / Year: 1988
Title: The Three-Dimensional Structure of Barley Serine Proteinase Inhibitor-2 in Solution as Determined by Proton Nuclear Magnetic Resonance Spectroscopy
Authors: Poulsen, F.M. / Kjaer, M. / Clore, G.M. / Gronenborn, A.M.
#4: Journal: Protein Eng. / Year: 1987
Title: The Determination of the Three-Dimensional Structure of Barley Serine Proteinase Inhibitor 2 by Nuclear Magnetic Resonance, Distance Geometry and Restrained Molecular Dynamics
Authors: Clore, G.M. / Gronenborn, A.M. / Kjaer, M. / Poulsen, F.M.
#5: Journal: Protein Eng. / Year: 1987
Title: Comparison of the Solution and X-Ray Structures of Barley Serine Proteinase Inhibitor 2
Authors: Clore, G.M. / Gronenborn, A.M. / James, M.N.G. / Kjaer, M. / Mcphalen, C.A. / Poulsen, F.M.
#6: Journal: Carlsberg Res.Commun. / Year: 1987
Title: Secondary Structure of Barley Serine Proteinase Inhibitor 2 Determined by Proton Nuclear Magnetic Resonance Spectroscopy
Authors: Kjaer, M. / Poulsen, F.M.
#7: Journal: Carlsberg Res.Commun. / Year: 1987
Title: Sequence Specific Assignment of the Proton Nuclear Magnetic Resonance Spectrum of Barley Serine Proteinase Inhibitor 2
Authors: Kjaer, M. / Ludvigsen, S. / Sorensen, O.W. / Denys, L.A. / Kindtler, J. / Poulsen, F.M.
History
DepositionSep 10, 1991Processing site: BNL
Revision 1.0Oct 31, 1993Provider: repository / Type: Initial release
Revision 1.1Mar 25, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CHYMOTRYPSIN INHIBITOR 2


Theoretical massNumber of molelcules
Total (without water)7,5481
Polymers7,5481
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein CHYMOTRYPSIN INHIBITOR 2


Mass: 7547.834 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Hordeum vulgare (barley) / References: UniProt: P01053

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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

NMR ensembleConformers submitted total number: 20

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