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- PDB-1bct: THREE-DIMENSIONAL STRUCTURE OF PROTEOLYTIC FRAGMENT 163-231 OF BA... -
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Basic information
Entry | Database: PDB / ID: 1bct | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF PROTEOLYTIC FRAGMENT 163-231 OF BACTERIOOPSIN DETERMINED FROM NUCLEAR MAGNETIC RESONANCE DATA IN SOLUTION | ||||||
![]() | BACTERIORHODOPSIN | ||||||
![]() | PHOTORECEPTOR | ||||||
Function / homology | ![]() photoreceptor activity / phototransduction / proton transmembrane transport / monoatomic ion channel activity / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Nolde, D.E. / Barsukov, I.L. / Lomize, A.L. / Arseniev, A.S. | ||||||
![]() | ![]() Title: Three-dimensional structure of proteolytic fragment 163-231 of bacterioopsin determined from nuclear magnetic resonance data in solution. Authors: Barsukov, I.L. / Nolde, D.E. / Lomize, A.L. / Arseniev, A.S. #1: ![]() Title: Sequence-Specific 1H (Slash)NMR Assignment and Conformation of Proteolytic Fragment 163-231 of Bacterioopsin Authors: Barsukov, I.L. / Abdulaeva, G.V. / Arseniev, A.S. / Bystrov, V.F. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 303.8 KB | Display | ![]() |
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PDB format | ![]() | 254.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 332.9 KB | Display | ![]() |
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Full document | ![]() | 383.3 KB | Display | |
Data in XML | ![]() | 14 KB | Display | |
Data in CIF | ![]() | 24.4 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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Atom site foot note | 1: MET 163 - ARG 164 MODEL 14 OMEGA =210.41 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | |||||||||
NMR ensembles |
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Components
#1: Protein | Mass: 7538.013 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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-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
NMR ensemble | Conformers submitted total number: 14 |
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