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- PDB-2nc8: NMR structure of the Mycobacterium tuberculosis LppM (Rv2171) pro... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2nc8 | ||||||
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Title | NMR structure of the Mycobacterium tuberculosis LppM (Rv2171) protein folded domain | ||||||
![]() | Lipoprotein LppM | ||||||
![]() | PROTEIN BINDING / TRANSPORT PROTEIN | ||||||
Function / homology | symbiont-mediated suppression of host innate immune response / cell wall / membrane => GO:0016020 / lipid binding / extracellular region / DUF3153 domain-containing protein / Protein LppM![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Barthe, P. / Cohen-Gonsaud, M. | ||||||
![]() | ![]() Title: Mycobacterium tuberculosis LppM Displays an Original Structure and Domain Composition Linked to a Dual Localization. Authors: Barthe, P. / Veyron-Churlet, R. / de Visch, A. / Gilleron, M. / Saliou, J.M. / Tomavo, S. / Nigou, J. / Brodin, P. / Cohen-Gonsaud, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.7 MB | Display | ![]() |
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PDB format | ![]() | 1.4 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 559.7 KB | Display | ![]() |
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Full document | ![]() | 950.2 KB | Display | |
Data in XML | ![]() | 125.4 KB | Display | |
Data in CIF | ![]() | 156.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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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: 19417.467 Da / Num. of mol.: 1 / Fragment: residues 26-185 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: lppM, AFL40_2254, BN1213_00992, BN1303_00406, ERS007661_00910, ERS007663_00966, ERS007665_02632, ERS007670_01654, ERS007672_03318, ERS007679_00953, ERS007681_03123, ERS007688_03112, ERS007720_ ...Gene: lppM, AFL40_2254, BN1213_00992, BN1303_00406, ERS007661_00910, ERS007663_00966, ERS007665_02632, ERS007670_01654, ERS007672_03318, ERS007679_00953, ERS007681_03123, ERS007688_03112, ERS007720_03717, ERS007722_01662, ERS013447_03488, ERS013471_03169, ERS023446_03335, ERS024213_03999, ERS027644_02995, ERS027653_02310, ERS027656_02172, ERS027666_01329, ERS031493_03859, ERS031537_04052, ERS075357_01597, ERS075361_03109, ERS075387_02172, ERS124361_03770, IQ38_09230, IQ40_08885, IQ42_08970, IQ45_08850, IQ47_08830, IQ48_08865, IU12_09440, IU13_08950, IU16_08915, IU17_08865, T209_08835 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: 6.8 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 / Details: DGSA-distance geometry simulated annealing | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 30 / Conformers submitted total number: 30 |