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- PDB-2n4b: EC-NMR Structure of Ralstonia metallidurans Rmet_5065 Determined ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2n4b | ||||||
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Title | EC-NMR Structure of Ralstonia metallidurans Rmet_5065 Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target CrR115 | ||||||
![]() | Uncharacterized protein | ||||||
![]() | Structural Genomics / Unknown Function / EC-NMR / AHSA1 / COG3832 / PF08327 / start domain / PSI-Biology / Northeast Structural Genomics Consortium / NESG | ||||||
Function / homology | Activator of Hsp90 ATPase homologue 1-like / Activator of Hsp90 ATPase homolog 1-like protein / START domain / Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4 / START-like domain superfamily / 2-Layer Sandwich / Alpha Beta / Activator of Hsp90 ATPase homologue 1-like C-terminal domain-containing protein![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Tang, Y. / Huang, Y.J. / Hopf, T.A. / Sander, C. / Marks, D. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
![]() | ![]() Title: Protein structure determination by combining sparse NMR data with evolutionary couplings. Authors: Tang, Y. / Huang, Y.J. / Hopf, T.A. / Sander, C. / Marks, D.S. / Montelione, G.T. | ||||||
History |
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Remark 0 | THIS ENTRY 2N4B REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN 2LCG DETERMINED ...THIS ENTRY 2N4B REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN 2LCG DETERMINED BY AUTHORS: T.A.RAMELOT,Y.YANG,D.WANG,C.CICCOSANTI,H.JANJUA,R.NAIR,T.B.ACTON,R.XIAO,J.K.EVERETT,G.T.MONTELIONE,M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 824.8 KB | Display | ![]() |
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PDB format | ![]() | 694.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 499.1 KB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 198.7 KB | Display | |
Data in CIF | ![]() | 125.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2n42C ![]() 2n44C ![]() 2n45C ![]() 2n46C ![]() 2n47C ![]() 2n48C ![]() 2n49C ![]() 2n4aC ![]() 2n4cC ![]() 2n4dC ![]() 2n4fC C: citing same article ( |
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Similar structure data | |
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: 16136.806 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: CH34 / ATCC 43123 / DSM 2839 / Gene: Rmet_5065 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR details | Text: Author used the experimental data from entry 2LCG. |
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Sample preparation
Sample | Conc.: 1.3 mM / Component: Rmet_5065-1 / Isotopic labeling: [U-100% 13C; U-100% 15N] |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: ReDCat were used to simulate 1 RDC data set from the reference structure. Protons from the Rosetta models were removed and added back using Reduce. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: lowest energy / Conformers calculated total number: 100 / Conformers submitted total number: 20 |