+Open data
-Basic information
Entry | Database: PDB / ID: 2mhk | ||||||
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Title | E. coli LpoA N-terminal domain | ||||||
Components | Penicillin-binding protein activator LpoA | ||||||
Keywords | PROTEIN BINDING / LpoA / TPR-like fold | ||||||
Function / homology | Function and homology information periplasmic side of cell outer membrane / enzyme regulator activity / peptidoglycan biosynthetic process / hydrolase activity, hydrolyzing O-glycosyl compounds / cell outer membrane / regulation of cell shape / periplasmic space / enzyme binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Jean, N.L. / Bougault, C. / Lodge, A. / Derouaux, A. / Callens, G. / Egan, A. / Lewis, R.J. / Vollmer, W. / Simorre, J. | ||||||
Citation | Journal: Structure / Year: 2014 Title: Elongated Structure of the Outer-Membrane Activator of Peptidoglycan Synthesis LpoA: Implications for PBP1A Stimulation. Authors: Jean, N.L. / Bougault, C.M. / Lodge, A. / Derouaux, A. / Callens, G. / Egan, A.J. / Ayala, I. / Lewis, R.J. / Vollmer, W. / Simorre, J.P. #1: Journal: To be Published Title: Backbone and side-chain 1H, 13C, 15N NMR assignment of the N-terminal domain of Escherichia coli LpoA Authors: Jean, N.L. / Bougault, C. / Lodge, A. / Derouaux, A. / Callens, G. / Egan, A. / Lewis, R.J. / Vollmer, W. / Simorre, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mhk.cif.gz | 1.6 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2mhk.ent.gz | 1.4 MB | Display | PDB format |
PDBx/mmJSON format | 2mhk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mh/2mhk ftp://data.pdbj.org/pub/pdb/validation_reports/mh/2mhk | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 28046.498 Da / Num. of mol.: 1 / Fragment: N-terminal domain (UNP residues 28-256) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: b3147, JW3116, lpoA, yraM / Plasmid: pET28 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P45464 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Ensemble of 20 NMR structures of E. coli LpoA N-terminal domain after refinement in water | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 2.0 mM [U-100% 13C; U-100% 15N] LpoA_n-ter, 100.0 mM CH3COOH/CH3COONa buffer, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.100 / pH: 4.500 / Pressure: ambient / Temperature: 323 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 5650 / NOE intraresidue total count: 1826 / NOE long range total count: 1018 / NOE medium range total count: 1225 / NOE sequential total count: 1141 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 213 / Protein psi angle constraints total count: 213 | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 700 / Conformers submitted total number: 20 |