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Yorodumi- PDB-2m5r: Solution structure of holo-acyl carrier protein of Leishmania major -
+Open data
-Basic information
Entry | Database: PDB / ID: 2m5r | ||||||
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Title | Solution structure of holo-acyl carrier protein of Leishmania major | ||||||
Components | Acyl carrier protein | ||||||
Keywords | LIPID BINDING PROTEIN | ||||||
Function / homology | Function and homology information acyl binding / acyl carrier activity / : / fatty acid biosynthetic process / mitochondrial matrix / mitochondrion Similarity search - Function | ||||||
Biological species | Leishmania major (eukaryote) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Authors | Kumar, A. / Surolia, A. / Sundd, M. | ||||||
Citation | Journal: To be Published Title: NMR structures of the apo- and holo- forms of the acyl carrier protein of Leishmania major Authors: Kumar, A. / Surolia, A. / Sundd, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2m5r.cif.gz | 504.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2m5r.ent.gz | 439.1 KB | Display | PDB format |
PDBx/mmJSON format | 2m5r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2m5r_validation.pdf.gz | 459 KB | Display | wwPDB validaton report |
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Full document | 2m5r_full_validation.pdf.gz | 780.8 KB | Display | |
Data in XML | 2m5r_validation.xml.gz | 112.7 KB | Display | |
Data in CIF | 2m5r_validation.cif.gz | 137.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m5/2m5r ftp://data.pdbj.org/pub/pdb/validation_reports/m5/2m5r | 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: 9005.208 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Leishmania major (eukaryote) / Gene: ACP, LMJF_27_0290 / Plasmid: pET 28 a(+) / Production host: Escherichia coli (E. coli) / References: UniProt: E9AD06 |
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#2: Chemical | ChemComp-PNS / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 20 mM [U-99% 13C; U-99% 15N] protein, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 20 mM / Component: protein-1 / Isotopic labeling: [U-99% 13C; U-99% 15N] |
Sample conditions | Ionic strength: 100 / pH: 6 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||
NMR constraints | NOE constraints total: 1956 / NOE intraresidue total count: 785 / NOE long range total count: 169 / NOE medium range total count: 398 / NOE sequential total count: 604 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 74 / Protein psi angle constraints total count: 74 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |