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Open data
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Basic information
Entry | Database: PDB / ID: 2hdl | ||||||
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Title | Solution structure of Brak/CXCL14 | ||||||
![]() | Small inducible cytokine B14 | ||||||
![]() | CYTOKINE / CXCL14 / Brak / chemokine | ||||||
Function / homology | ![]() positive regulation of natural killer cell chemotaxis / negative regulation of myoblast differentiation / chemokine activity / inner ear development / chemotaxis / antimicrobial humoral immune response mediated by antimicrobial peptide / cell-cell signaling / killing of cells of another organism / Golgi apparatus / signal transduction / extracellular space Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT, ITERATIVE NOE REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR DYNAMICS IN EXPLICIT SOLVEN | ||||||
![]() | Peterson, F.C. / Thorpe, J.A. / Harder, A.G. / Volkman, B.F. / Schwarze, S.R. | ||||||
![]() | ![]() Title: Structural Determinants Involved in the Regulation of CXCL14/BRAK Expression by the 26 S Proteasome. Authors: Peterson, F.C. / Thorpe, J.A. / Harder, A.G. / Volkman, B.F. / Schwarze, S.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 570 KB | Display | ![]() |
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PDB format | ![]() | 485.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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: 9500.201 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: ALL TRIPLE-RESONANCE AND NOESY SPECTRA WERE ACQUIRED USING A CRYOGENIC PROBE |
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Sample preparation
Details | Contents: 1 mM CXCL14 U-15N, 13C; 100mM phosphate buffer, 150mM NaCl,95% H2O, 5% D2O Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 300 mM / pH: 6.5 / 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 | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT, ITERATIVE NOE REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR DYNAMICS IN EXPLICIT SOLVEN Software ordinal: 1 Details: STRUCTURES ARE BASED ON A TOTAL OF 894 NOE CONSTRAINTS ( 366 INTRA, 186 SEQUENTIAL, 133 MEDIUM and 209 LONG RANGE CONSTRAINTS) AND 97 PHI AND PSI DIHEDRAL ANGLE CONSTRAINTS. | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |