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Yorodumi- PDB-1xpn: NMR structure of P. aeruginosa protein PA1324: Northeast Structur... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1xpn | ||||||
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Title | NMR structure of P. aeruginosa protein PA1324: Northeast Structural Genomics Consortium target PaP1 | ||||||
Components | hypothetical protein PA1324 | ||||||
Keywords | STRUCTURAL GENOMICS / UNKNOWN FUNCTION / b-barrel / Northeast Structural Genomics Consortium / NESG / Protein Structure Initiative / PSI | ||||||
Function / homology | Prokaryotic membrane lipoprotein lipid attachment site profile. / Carboxypeptidase regulatory-like domain-containing protein Function and homology information | ||||||
Biological species | Pseudomonas aeruginosa (bacteria) | ||||||
Method | SOLUTION NMR / Molecular Dynamics, Simulated Annealing | ||||||
Authors | Cort, J.R. / Ni, S. / Lockert, E.E. / Montelione, G.T. / Kennedy, M.A. / Northeast Structural Genomics Consortium (NESG) | ||||||
Citation | Journal: Protein Sci. / Year: 2009 Title: Structure and function of Pseudomonas aeruginosa protein PA1324 (21-170). Authors: Mercier, K.A. / Cort, J.R. / Kennedy, M.A. / Lockert, E.E. / Ni, S. / Shortridge, M.D. / Powers, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xpn.cif.gz | 986.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xpn.ent.gz | 826.3 KB | Display | PDB format |
PDBx/mmJSON format | 1xpn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1xpn_validation.pdf.gz | 342.7 KB | Display | wwPDB validaton report |
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Full document | 1xpn_full_validation.pdf.gz | 470.7 KB | Display | |
Data in XML | 1xpn_validation.xml.gz | 63.1 KB | Display | |
Data in CIF | 1xpn_validation.cif.gz | 83.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xp/1xpn ftp://data.pdbj.org/pub/pdb/validation_reports/xp/1xpn | 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: 18403.201 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Strain: PAO1 / Gene: PA1324 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9I420 |
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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 conditions | Ionic strength: 300 mM NaCl / pH: 6.8 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: Molecular Dynamics, Simulated Annealing / Software ordinal: 1 Details: NOE distance restraints were determined automatically using AutoStructure (G.T. Montelione & Y.J. Huang) starting from peak-picked NOESY data and chemical shift assignments. Final refinement ...Details: NOE distance restraints were determined automatically using AutoStructure (G.T. Montelione & Y.J. Huang) starting from peak-picked NOESY data and chemical shift assignments. Final refinement was conducted in explicit solvent with Leonard-Jones and electrostatic potentials. Residues 1-26 are unrestrained and constitute a flexible, n-terminal tail. The structure of residues 27-170 is restrained by 1861 noe distance restraints (541 intraresidue, 513 sequential, 190 medium range, and 617 long range (n>4)), 132 dihedral restraints (65 phi, 67 psi), and 70 h-bond restraints (for 35 h-bonds). Dihedral restraints were derived from Talos and HNHA. H-bond restraints were derived from analysis of amides that exchange slowly with D2O solvent together with initial structures derived from Noesy data. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy, fewest violations, closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy,structures with the fewest restraint violations Conformers calculated total number: 20 / Conformers submitted total number: 20 |