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Open data
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Basic information
Entry | Database: PDB / ID: 5t43 | ||||||
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Title | NMR Structure of Apo-form Human Tear Lipocalin | ||||||
![]() | Lipocalin-1 | ||||||
![]() | TRANSPORT PROTEIN | ||||||
Function / homology | ![]() Transport of fatty acids / response to stimulus / chloride ion binding / cysteine-type endopeptidase inhibitor activity / sensory perception of taste / signaling receptor binding / proteolysis / extracellular space / zinc ion binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Vogel, H.J. / Liu, Z. | ||||||
Funding support | ![]()
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![]() | ![]() Title: NMR Structure of Apo-form Human Tear Lipocalin Authors: Vogel, H.J. / Liu, Z. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 942 KB | Display | ![]() |
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PDB format | ![]() | 788.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 409 KB | Display | ![]() |
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Full document | ![]() | 604 KB | Display | |
Data in XML | ![]() | 75.2 KB | Display | |
Data in CIF | ![]() | 97.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 17453.652 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() References: UniProt: P31025 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 1.0 mM [U-99% 13C; U-99% 15N] Lipocalin, 90 % H2O, 10 % D2O, 50 mM sodium phosphate, 0.04 % sodium azide, 90% H2O/10% D2O Label: 15N/13C_sample / Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample |
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Sample conditions | Details: 50 mM NaPi, pH 7.4 / Ionic strength: 50 mM / Label: conditions_1 / pH: 7.4 / Pressure: 1 atm / Temperature: 310 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: simulated annealing / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 5000 / Conformers submitted total number: 20 |