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- PDB-1gm2: The independent structure of the antitryptic reactive site loop o... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gm2 | ||||||
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Title | The independent structure of the antitryptic reactive site loop of Bowman-Birk inhibitor and sunflower trypsin inhibitor-1 | ||||||
![]() | BOWMAN-BIRK INHIBITOR DERIVED PEPTIDE | ||||||
![]() | HYDROLASE INHIBITOR / BOWMAN-BIRK INHIBITOR PROTEIN MIMETIC / SUNFLOWER TRYPSIN INHIBITOR-1 (SFTI-1) MIMETIC / TRYPSIN INHIBITOR / TYPE VIB BETA-TURN PEPTIDE | ||||||
Function / homology | Bowman-Birk serine protease inhibitor family / Bowman-Birk serine protease inhibitors family signature. / Proteinase inhibitor I12, Bowman-Birk / Bowman-Birk type proteinase inhibitor / Bowman-Birk type proteinase inhibitor / serine-type endopeptidase inhibitor activity / extracellular region / Bowman-Birk type proteinase inhibitor DE-4![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Brauer, A.B.E. / Kelly, G. / Matthews, S.J. / Leatherbarrow, R.J. | ||||||
![]() | ![]() Title: The (1)H-NMR solution structure of the antitryptic core peptide of Bowman-Birk inhibitor proteins: a minimal canonical loop. Authors: Brauer, A.B. / Kelly, G. / Matthews, S.J. / Leatherbarrow, R.J. #1: Journal: Biochemistry / Year: 2002 Title: A Conserved Cis Peptide Bond is Necessary for the Activity of Bowman-Birk Inhibitor Protein Authors: Brauer, A.B.E. / Domingo, G.J. / Cooke, R.M. / Matthews, S.J. / Leatherbarrow, R.J. #2: ![]() Title: The Bowman-Birk Inhibitor Reactive Site Loop Represents an Independent Structural Beta-Hairpin Motif Authors: Brauer, A.B.E. / Kelly, G. / Mcbride, J.D. / Cooke, R.M. / Matthews, S.J. / Leatherbarrow, R.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.5 KB | Display | ![]() |
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PDB format | ![]() | 64.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 334.3 KB | Display | ![]() |
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Full document | ![]() | 460.4 KB | Display | |
Data in XML | ![]() | 5.7 KB | Display | |
Data in CIF | ![]() | 9.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: 1227.430 Da / Num. of mol.: 1 / Fragment: ANTITRYPTIC REACTIVE SITE LOOP / Mutation: YES / Source method: obtained synthetically Source: (synth.) ![]() References: UniProt: P01059 |
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Compound details | TERMINAL RESIDUES ARE MUTATED REALTIVE TO WILD TYPE SEQUENCE |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING 1H-NMR. |
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Sample preparation
Sample conditions | pH: 3.8 / Temperature: 298 K |
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-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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Processing
NMR software | Name: ![]() |
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Refinement | Method: simulated annealing / Software ordinal: 1 |
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 300 / Conformers submitted total number: 30 |