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- PDB-2vbx: Feast or famine regulatory protein (Rv3291c)from M. tuberculosis ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2vbx | ||||||
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Title | Feast or famine regulatory protein (Rv3291c)from M. tuberculosis complexed with L-Phenylalanine | ||||||
![]() | TRANSCRIPTIONAL REGULATORY PROTEIN | ||||||
![]() | DNA BINDING PROTEIN / FEAST/FAMINE REGULATORY PROTEIN / DNA-BINDING PROTEIN / TRANSCRIPTION REGULATOR / TRANSCRIPTION REGULATION / M. TUBERCULOSIS / HISTIDINE COMPLEX / LRP / RV3291C / DNA-BINDING / TRANSCRIPTION | ||||||
Function / homology | ![]() amino acid binding / response to amino acid / protein homooligomerization / sequence-specific DNA binding / DNA binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Shrivastava, T. / Ramachandran, R. | ||||||
![]() | ![]() Title: Mechanistic Insights from the Crystal Structures of a Feast/Famine Regulatory Protein from Mycobacterium Tuberculosis H37Rv. Authors: Shrivastava, T. / Ramachandran, R. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 66.9 KB | Display | ![]() |
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PDB format | ![]() | 51.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 437.9 KB | Display | ![]() |
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Full document | ![]() | 452.4 KB | Display | |
Data in XML | ![]() | 15.1 KB | Display | |
Data in CIF | ![]() | 19.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2ivmC ![]() 2vbwC ![]() 2vbyC ![]() 2vbzC ![]() 2vc0C ![]() 2vc1C C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 16530.596 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Nonpolymer details | L-HISTIDINE (HIS): L-HISTIDINE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.94 Å3/Da / Density % sol: 68.52 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.75→20 Å / Num. obs: 13598 / % possible obs: 98.6 % / Observed criterion σ(I): 2 / Redundancy: 5.5 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 13.7 |
Reflection shell | Resolution: 2.75→2.9 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 2.9 / % possible all: 99.7 |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 2.75→71.43 Å / Cor.coef. Fo:Fc: 0.896 / Cor.coef. Fo:Fc free: 0.869 / Cross valid method: THROUGHOUT / ESU R: 0.269 / ESU R Free: 0.321 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-3 ARE DISORDERED IN THE STRUCTURE
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||
Displacement parameters | Biso mean: 36.83 Å2
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Refinement step | Cycle: LAST / Resolution: 2.75→71.43 Å
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LS refinement shell | Resolution: 2.75→2.82 Å / Total num. of bins used: 20 /
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