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- PDB-1xax: NMR structure of HI0004, a putative essential gene product from H... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xax | ||||||
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Title | NMR structure of HI0004, a putative essential gene product from Haemophilus influenzae | ||||||
![]() | Hypothetical UPF0054 protein HI0004 | ||||||
![]() | structural genomics / unknown function / Haemophilus influenzae / MMP / hydrolase / protein structure initiative / S2F / Structure 2 Function Project | ||||||
Function / homology | ![]() RNA endonuclease activity / metalloendopeptidase activity / rRNA processing / Hydrolases; Acting on ester bonds / zinc ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, torsion angle dynamics | ||||||
![]() | Yeh, D.C. / Parsons, J.F. / Parsons, L.M. / Liu, F. / Eisenstein, E. / Orban, J. / Structure 2 Function Project (S2F) | ||||||
![]() | ![]() Title: NMR structure of HI0004, a putative essential gene product from Haemophilus influenzae, and comparison with the X-ray structure of an Aquifex aeolicus homolog Authors: Yeh, D.C. / Parsons, L.M. / Parsons, J.F. / Liu, F. / Eisenstein, E. / Orban, J. #1: Journal: J.Biomol.NMR / Year: 2004 Title: NMR assignment of the hypothetical protein HI0004 from Haemophilus Influenzae - a putative essential gene product Authors: Yeh, D.C. / Parsons, J.F. / Parsons, L.M. / Liu, F. / Eisenstein, E. / Orban, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 816 KB | Display | ![]() |
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PDB format | ![]() | 685.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 344.4 KB | Display | ![]() |
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Full document | ![]() | 597.5 KB | Display | |
Data in XML | ![]() | 77.9 KB | Display | |
Data in CIF | ![]() | 100.7 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: 17369.334 Da / Num. of mol.: 1 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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NMR details | Text: NH residual dipolar coupling were used for validation of structure |
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Sample preparation
Details | Contents: 1mM U-15N,13C hi0004, 50mM phosphate buffer, 10mM NaCl Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 50mM phosphate, 100mM NaCl / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing, torsion angle dynamics Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |