+Open data
-Basic information
Entry | Database: PDB / ID: 2n59 | ||||||
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Title | Solution Structure of R. palustris CsgH | ||||||
Components | Putative uncharacterized protein CsgH | ||||||
Keywords | UNKNOWN FUNCTION | ||||||
Function / homology | : / : / CsgH protein / : / Immunoglobulin-like - #2420 / Immunoglobulin-like / Sandwich / Mainly Beta / CsgH-like domain-containing protein Function and homology information | ||||||
Biological species | Rhodopseudomonas palustris DX-1 (phototrophic) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Hawthorne, W.J. / Taylor, J.D. / Escalera-Maurer, A. / Lambert, S. / Koch, M. / Scull, N. / Sefer, L. / Xu, Y. / Matthews, S.J. | ||||||
Citation | Journal: Sci Rep / Year: 2016 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n59.cif.gz | 618.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n59.ent.gz | 542.6 KB | Display | PDB format |
PDBx/mmJSON format | 2n59.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2n59_validation.pdf.gz | 407 KB | Display | wwPDB validaton report |
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Full document | 2n59_full_validation.pdf.gz | 548.2 KB | Display | |
Data in XML | 2n59_validation.xml.gz | 35.4 KB | Display | |
Data in CIF | 2n59_validation.cif.gz | 60 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n5/2n59 ftp://data.pdbj.org/pub/pdb/validation_reports/n5/2n59 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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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.) Rhodopseudomonas palustris DX-1 (phototrophic) Strain: DX-1 / Gene: csgH, Rpdx1_1250 / Plasmid: pET28 / Production host: Escherichia coli (E. coli) / Strain (production host): SHuffle T7 Express / References: UniProt: E6VF87 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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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
NMR software |
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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 |