[English] 日本語
Yorodumi- PDB-6d10: CS-rosetta determined structures of the C-terminal domain of AlgF... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6d10 | ||||||
---|---|---|---|---|---|---|---|
Title | CS-rosetta determined structures of the C-terminal domain of AlgF from P. aeruginosa | ||||||
Components | Alginate biosynthesis protein AlgF | ||||||
Keywords | CELL ADHESION / Carbohydrate acetylation EPS export | ||||||
Function / homology | alginic acid acetylation / Alginate O-acetyl transferase AlgF / Alginate O-acetyl transferase AlgF / alginic acid biosynthetic process / periplasmic space / Alginate biosynthesis protein AlgF Function and homology information | ||||||
Biological species | Pseudomonas aeruginosa (bacteria) | ||||||
Method | SOLUTION NMR / SOLUTION SCATTERING / molecular dynamics | ||||||
Authors | Tammam, S. / Howell, P.L. | ||||||
Funding support | Canada, 1items
| ||||||
Citation | Journal: To Be Published Title: Pseudomonas aeruginosa AlgF is an adaptor protein required for acetylation of the alginate exopolysaccharide Authors: Low, K.E. / Tammam, S.D. / Whitfield, G.B. / Riley, L.M. / Weadge, J.T. / Caldwell, S.J. / Baker, P. / Chong, P.A. / Walvoort, M.T.C. / Kitova, E.N. / Grant, T.D. / Snell, E.H. / Klassen, J. ...Authors: Low, K.E. / Tammam, S.D. / Whitfield, G.B. / Riley, L.M. / Weadge, J.T. / Caldwell, S.J. / Baker, P. / Chong, P.A. / Walvoort, M.T.C. / Kitova, E.N. / Grant, T.D. / Snell, E.H. / Klassen, J.S. / Codee, J.D.C. / Howell, P.L. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 6d10.cif.gz | 287.2 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb6d10.ent.gz | 230.8 KB | Display | PDB format |
PDBx/mmJSON format | 6d10.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6d10_validation.pdf.gz | 508 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 6d10_full_validation.pdf.gz | 548.8 KB | Display | |
Data in XML | 6d10_validation.xml.gz | 15.3 KB | Display | |
Data in CIF | 6d10_validation.cif.gz | 36.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d1/6d10 ftp://data.pdbj.org/pub/pdb/validation_reports/d1/6d10 | HTTPS FTP |
-Related structure data
Related structure data | 6cztC C: citing same article (ref.) |
---|---|
Similar structure data | |
Other databases |
|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 20917.729 Da / Num. of mol.: 1 / Fragment: residues 30-216 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (bacteria) Strain: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 Gene: algF, PA3550 / Plasmid: pET24b / Production host: Escherichia coli (E. coli) / Variant (production host): CodonPlus / References: UniProt: Q06062 |
---|
-Experimental details
-Experiment
Experiment |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Type: solution Contents: 1 mM [U-13C; U-15N] AlgF, 50 mM potassium phosphate, 2 % v/v glycerol, 10 mM DTT, 90% H2O/10% D2O Details: Uniformly labeled 15N and 13C AlgF / Label: AlgF_CTD / Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||||||
Sample conditions | Ionic strength: 0.05 M / Label: AlgF_NMR / pH: 6.8 / Pressure: 1 atm / Temperature: 298 K |
-Data collection
NMR spectrometer |
|
---|
-Processing
NMR software |
| |||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: molecular dynamics / Software ordinal: 5 | |||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 3000 / Conformers submitted total number: 10 |