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Yorodumi- PDB-2n6g: Solution structure of an MbtH-like protein from Mycobacterium avi... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2n6g | ||||||
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Title | Solution structure of an MbtH-like protein from Mycobacterium avium, Seattle Structural Genomics Center for Infectious Disease target MyavA.01649.c | ||||||
Components | MbtH-like protein | ||||||
Keywords | UNKNOWN FUNCTION / SSGCID / tuberculosis / infectious diseases / mbtH-like / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease | ||||||
Function / homology | MbtH-like protein / MbtH-like domain / MbtH-like domain superfamily / MbtH-like protein / MbtH-like protein / Conserved domain protein Function and homology information | ||||||
Biological species | Mycobacterium avium 104 (bacteria) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | closest to the average, model1 | ||||||
Authors | Buchko, G.W. / Seattle Structural Genomics Center for Infectious Disease (SSGCID) | ||||||
Citation | Journal: To be Published Title: Solution structure of a MbtH-like protein from Mycobacterium avium. Authors: Buchko, G.W. / Hewitt, S.N. / Van Voorhis, W.C. / Myler, P.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n6g.cif.gz | 535.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n6g.ent.gz | 454 KB | Display | PDB format |
PDBx/mmJSON format | 2n6g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2n6g_validation.pdf.gz | 538.1 KB | Display | wwPDB validaton report |
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Full document | 2n6g_full_validation.pdf.gz | 688.6 KB | Display | |
Data in XML | 2n6g_validation.xml.gz | 34.7 KB | Display | |
Data in CIF | 2n6g_validation.cif.gz | 51 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n6/2n6g ftp://data.pdbj.org/pub/pdb/validation_reports/n6/2n6g | 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: 8994.837 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium avium 104 (bacteria) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: A0A0H2ZVT0*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The sample was not very stable and multiple samples were made (same conditions) to collect the data. |
-Sample preparation
Details | Contents: 100 mM sodium chloride, 20 mM TRIS, 1 mM DTT, 93% H2O/7% D2O Solvent system: 93% H2O/7% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.12 / pH: 7 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 Details: STRUCTURE DETERMINATION WAS PERFORMED ITERATIVELY USING CYANA (AUTOMATED NOESY ASSIGNMENTS). A TOTAL OF 20 STRUCTURES OUT OF 100 WITH LOWEST TARGET FUNCTION FROM THE FINAL CYANA CALCULATION ...Details: STRUCTURE DETERMINATION WAS PERFORMED ITERATIVELY USING CYANA (AUTOMATED NOESY ASSIGNMENTS). A TOTAL OF 20 STRUCTURES OUT OF 100 WITH LOWEST TARGET FUNCTION FROM THE FINAL CYANA CALCULATION WERE TAKEN AND REFINED BY RESTRAINED MOLECULAR DYNAMICS/ENERGY MINIMIZATION IN EXPLICIT WATER (CNS) AFTER ADDING 0% TO THE UPPER BOUNDARY LIMIT OF THE DISTANCE RESTRAINTS AND THE VDW LIMIT TO THE LOWER RESTRAINT. PARAM19 WAS USED FOR THE WATER REFINEMENT CALCULATIONS. | ||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 357 / Protein phi angle constraints total count: 36 / Protein psi angle constraints total count: 36 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |