+Open data
-Basic information
Entry | Database: PDB / ID: 1gyf | ||||||
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Title | GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN | ||||||
Components | PROTEIN (CYTOPLASMIC DOMAIN BINDING PROTEIN (CD2BP2)) | ||||||
Keywords | IMMUNE SYSTEM / T CELL SIGNALING / PROLINE-RICH SEQUENCE RECOGNITION / ADAPTER DOMAIN | ||||||
Function / homology | Function and homology information spliceosomal tri-snRNP complex assembly / U5 snRNP / ribonucleoprotein complex binding / fibrillar center / nuclear speck / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
Authors | Freund, C. / Doetsch, V. / Nishizawa, K. / Reinherz, E.L. / Wagner, G. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1999 Title: The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. Authors: Freund, C. / Dotsch, V. / Nishizawa, K. / Reinherz, E.L. / Wagner, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gyf.cif.gz | 308.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gyf.ent.gz | 255.4 KB | Display | PDB format |
PDBx/mmJSON format | 1gyf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gy/1gyf ftp://data.pdbj.org/pub/pdb/validation_reports/gy/1gyf | 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: 7320.014 Da / Num. of mol.: 1 / Fragment: CD2-BINDING DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell: T-LYMPHOCYTE / Plasmid: PTFT74 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O95400 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: LOWEST ENERGY. NULL |
-Sample preparation
Details | Contents: 90% WATER/10%D2O |
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Sample conditions | Ionic strength: 50 mM NAPO4 / pH: 6.3 / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATIONS, LEAST ENERGY FUNCTION Conformers calculated total number: 30 / Conformers submitted total number: 16 |