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Open data
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Basic information
Entry | Database: PDB / ID: 2n59 | ||||||
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Title | Solution Structure of R. palustris CsgH | ||||||
![]() | Putative uncharacterized protein CsgH | ||||||
![]() | UNKNOWN FUNCTION | ||||||
Function / homology | Immunoglobulin-like - #2420 / Immunoglobulin-like / Sandwich / Mainly Beta / Uncharacterized protein![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Hawthorne, W.J. / Taylor, J.D. / Escalera-Maurer, A. / Lambert, S. / Koch, M. / Scull, N. / Sefer, L. / Xu, Y. / Matthews, S.J. | ||||||
![]() | ![]() Title: Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones. Authors: Taylor, J.D. / Hawthorne, W.J. / Lo, J. / Dear, A. / Jain, N. / Meisl, G. / Andreasen, M. / Fletcher, C. / Koch, M. / Darvill, N. / Scull, N. / Escalera-Maurer, A. / Sefer, L. / Wenman, R. / ...Authors: Taylor, J.D. / Hawthorne, W.J. / Lo, J. / Dear, A. / Jain, N. / Meisl, G. / Andreasen, M. / Fletcher, C. / Koch, M. / Darvill, N. / Scull, N. / Escalera-Maurer, A. / Sefer, L. / Wenman, R. / Lambert, S. / Jean, J. / Xu, Y. / Turner, B. / Kazarian, S.G. / Chapman, M.R. / Bubeck, D. / de Simone, A. / Knowles, T.P. / Matthews, S.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 | ![]() | 618.2 KB | Display | ![]() |
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PDB format | ![]() | 542.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 407 KB | Display | ![]() |
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Full document | ![]() | 548.2 KB | Display | |
Data in XML | ![]() | 35.4 KB | Display | |
Data in CIF | ![]() | 60 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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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 | Mass: 11183.521 Da / Num. of mol.: 1 / Fragment: UNP residues 10-106 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: DX-1 / Gene: csgH, Rpdx1_1250 / Plasmid: pET28 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 150 / pH: 6.5 / Pressure: ambient / Temperature: 292 K |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1721 / NOE intraresidue total count: 575 / NOE long range total count: 373 / NOE medium range total count: 54 / NOE sequential total count: 200 / Disulfide bond constraints total count: 1 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 85 / Protein psi angle constraints total count: 85 | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 300 / Conformers submitted total number: 20 / Representative conformer: 1 |