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Open data
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Basic information
Entry | Database: PDB / ID: 1cir | ||||||
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Title | COMPLEX OF TWO FRAGMENTS OF CI2 [(1-40)(DOT)(41-64)] | ||||||
![]() | (CHYMOTRYPSIN INHIBITOR 2) x 2 | ||||||
![]() | SERINE PROTEASE INHIBITOR | ||||||
Function / homology | Proteinase inhibitor I13, potato inhibitor I / Proteinase inhibitor I13, potato inhibitor I superfamily / Potato inhibitor I family / Potato inhibitor I family signature. / serine-type endopeptidase inhibitor activity / response to wounding / Subtilisin-chymotrypsin inhibitor-2A![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Davis, B.J. / Fersht, A.R. | ||||||
![]() | ![]() Title: Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary ...Title: Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanism Authors: Neira, J.L. / Davis, B. / Ladurner, A.G. / Buckle, A.M. / Gay Gde, P. / Fersht, A.R. #1: ![]() Title: The Structure of the Transition State for the Association of Two Fragments of the Barley Chymotrypsin Inhibitor-2 to Generate Native-Like Protein: Implications for Mechanisms of Protein Folding Authors: De Prat Gay, G. / Ruiz-Sanz, J. / Davis, B. / Fersht, A.R. #2: ![]() Title: Generation of a Family of Protein Fragments for Structure-Folding Studies. 1. Folding Complementation of Two Fragments of Chymotrypsin Inhibitor-2 Formed by Cleavage at its Unique Methionine Residue Authors: De Prat Gay, G. / Fersht, A.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 409.4 KB | Display | ![]() |
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PDB format | ![]() | 339.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 353 KB | Display | ![]() |
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Full document | ![]() | 650.9 KB | Display | |
Data in XML | ![]() | 44.8 KB | Display | |
Data in CIF | ![]() | 67.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 4424.221 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: CLEAVED BETWEEN RESIDUES 40 AND 41 / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 2877.325 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: CLEAVED BETWEEN RESIDUES 40 AND 41 / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
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NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 20 |