+Open data
-Basic information
Entry | Database: PDB / ID: 5t43 | ||||||
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Title | NMR Structure of Apo-form Human Tear Lipocalin | ||||||
Components | Lipocalin-1 | ||||||
Keywords | TRANSPORT PROTEIN | ||||||
Function / homology | Function and homology information Transport of fatty acids / 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 | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Vogel, H.J. / Liu, Z. | ||||||
Funding support | Canada, 1items
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Citation | Journal: To Be Published 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5t43.cif.gz | 942 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5t43.ent.gz | 788.8 KB | Display | PDB format |
PDBx/mmJSON format | 5t43.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5t43_validation.pdf.gz | 409 KB | Display | wwPDB validaton report |
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Full document | 5t43_full_validation.pdf.gz | 604 KB | Display | |
Data in XML | 5t43_validation.xml.gz | 75.2 KB | Display | |
Data in CIF | 5t43_validation.cif.gz | 97.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t4/5t43 ftp://data.pdbj.org/pub/pdb/validation_reports/t4/5t43 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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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.) Homo sapiens (human) / Gene: LCN1, VEGP Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) 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 |