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Open data
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Basic information
Entry | Database: PDB / ID: 1rw5 | ||||||
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Title | Solution structure of human prolactin | ||||||
![]() | Prolactin | ||||||
![]() | HORMONE/GROWTH FACTOR / Four helix bundle / cytokine / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | ![]() prolactin receptor binding / positive regulation of lactation / prolactin signaling pathway / mammary gland development / Prolactin receptor signaling / negative regulation of endothelial cell proliferation / Growth hormone receptor signaling / lactation / negative regulation of angiogenesis / response to nutrient levels ...prolactin receptor binding / positive regulation of lactation / prolactin signaling pathway / mammary gland development / Prolactin receptor signaling / negative regulation of endothelial cell proliferation / Growth hormone receptor signaling / lactation / negative regulation of angiogenesis / response to nutrient levels / endosome lumen / female pregnancy / positive regulation of receptor signaling pathway via JAK-STAT / hormone activity / positive regulation of miRNA transcription / positive regulation of canonical NF-kappaB signal transduction / cell surface receptor signaling pathway / Amyloid fiber formation / positive regulation of cell population proliferation / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Teilum, K. / Hoch, J. / Martial, J.A. / Kragelund, B.B. | ||||||
![]() | ![]() Title: Solution structure of human prolactin Authors: Teilum, K. / Hoch, J.C. / Goffin, V. / Kinet, S. / Martial, J.A. / Kragelund, B.B. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.2 MB | Display | ![]() |
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PDB format | ![]() | 1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 351.6 KB | Display | ![]() |
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Full document | ![]() | 535.6 KB | Display | |
Data in XML | ![]() | 87.1 KB | Display | |
Data in CIF | ![]() | 111.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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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: 22929.195 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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Sample preparation
Details |
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Sample conditions | Ionic strength: 0 / pH: 8.05 / Pressure: ambient / Temperature: 310 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: simulated annealing / Software ordinal: 1 Details: The structures are based on 2149 NOE distance contraints, 320 dihedral angle constraints, and 81 residual dipolar couplings | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: The submitted conformer models are the 20 with the lowest energy of the structures with no restraint violations larger than 0.4 A, 5 deg, and 1 Hz for noe's, torsion ...Conformer selection criteria: The submitted conformer models are the 20 with the lowest energy of the structures with no restraint violations larger than 0.4 A, 5 deg, and 1 Hz for noe's, torsion angles and rdc's respectively Conformers calculated total number: 200 / Conformers submitted total number: 20 |