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Yorodumi- PDB-1blr: NMR SOLUTION STRUCTURE OF HUMAN CELLULAR RETINOIC ACID BINDING PR... -
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-Basic information
Entry | Database: PDB / ID: 1blr | ||||||
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Title | NMR SOLUTION STRUCTURE OF HUMAN CELLULAR RETINOIC ACID BINDING PROTEIN-TYPE II, 22 STRUCTURES | ||||||
Components | CELLULAR RETINOIC ACID BINDING PROTEIN-TYPE II | ||||||
Keywords | TRANSPORT / CRABPII / VITAMIN A | ||||||
Function / homology | Function and homology information positive regulation of collateral sprouting / retinoid binding / retinal binding / retinoic acid binding / embryonic forelimb morphogenesis / retinoic acid metabolic process / retinol binding / Signaling by Retinoic Acid / epidermis development / fatty acid transport ...positive regulation of collateral sprouting / retinoid binding / retinal binding / retinoic acid binding / embryonic forelimb morphogenesis / retinoic acid metabolic process / retinol binding / Signaling by Retinoic Acid / epidermis development / fatty acid transport / cyclin binding / fatty acid binding / regulation of DNA-templated transcription / signal transduction / endoplasmic reticulum / extracellular exosome / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / DGSA | ||||||
Authors | Wang, L. / Li, Y. / Abilddard, F. / Yan, H. / Markely, J. | ||||||
Citation | Journal: Biochemistry / Year: 1998 Title: NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding. Authors: Wang, L. / Li, Y. / Abildgaard, F. / Markley, J.L. / Yan, H. #1: Journal: Structure / Year: 1994 Title: Crystal Structures of Cellular Retinoic Acid Binding Proteins I and II in Complex with All-Trans-Retinoic Acid and a Synthetic Retinoid Authors: Kleywegt, G.J. / Bergfors, T. / Senn, H. / Le Motte, P. / Gsell, B. / Shudo, K. / Jones, T.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1blr.cif.gz | 940.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1blr.ent.gz | 783.9 KB | Display | PDB format |
PDBx/mmJSON format | 1blr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bl/1blr ftp://data.pdbj.org/pub/pdb/validation_reports/bl/1blr | HTTPS FTP |
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-Related structure data
Similar structure data |
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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: 15581.802 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line: BL21 (DE3)/PLYSS / Gene: CRABP-II / Plasmid: PET17B/PLYSS / Species (production host): Escherichia coli / Cell line (production host): BL21 (DE3)/PLYSS / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P29373 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: MODEL 1 - THE RESONANCES WERE DETERMINED BY MEANS OF TRIPLE-RESONANCE NMR EXPERIMENTS ON 13C, 15N-LABELED CRABPII |
-Sample preparation
Details | Contents: H2O |
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Sample conditions | pH: 7.3 / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
Software |
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NMR software |
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Refinement | Method: DGSA / Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 70 / Conformers submitted total number: 22 |