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- PDB-2kln: Solution Structure of STAS domain of RV1739c from M. tuberculosis -
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Open data
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Basic information
Entry | Database: PDB / ID: 2kln | ||||||
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Title | Solution Structure of STAS domain of RV1739c from M. tuberculosis | ||||||
![]() | PROBABLE SULPHATE-TRANSPORT TRANSMEMBRANE PROTEIN, COG0659 | ||||||
![]() | TRANSPORT PROTEIN / SLC26 / Sulfate / SulP / AntiSigma Factor Antagonist / ensemble of 25 structures / Membrane / Transmembrane | ||||||
Function / homology | STAS domain / Transcription Regulator spoIIAA / 2-Layer Sandwich / Alpha Beta / : ![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics, DGSA-distance geometry simulated annealing | ||||||
![]() | Sharma, A.K. / Ye, L. / Zolotarev, A.S. / Alper, S.L. / Rigby, A.C. | ||||||
![]() | ![]() Title: Solution Structure of the Guanine Nucleotide-binding STAS Domain of SLC26-related SulP Protein Rv1739c from Mycobacterium tuberculosis. Authors: Sharma, A.K. / Ye, L. / Baer, C.E. / Shanmugasundaram, K. / Alber, T. / Alper, S.L. / Rigby, A.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.1 MB | Display | ![]() |
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PDB format | ![]() | 949.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 345.5 KB | Display | ![]() |
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Full document | ![]() | 577.5 KB | Display | |
Data in XML | ![]() | 73.9 KB | Display | |
Data in CIF | ![]() | 97.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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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: 15093.152 Da / Num. of mol.: 1 / Fragment: residues 437-560 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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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: 275 / pH: 7.2 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics, DGSA-distance geometry simulated annealing Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 400 / Conformers submitted total number: 25 |