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Yorodumi- PDB-6lr2: SOLUTION STRUCTURE OF THE YTH DOMAIN IN YTH DOMAIN-2 CONTAINING P... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6lr2 | ||||||
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Title | SOLUTION STRUCTURE OF THE YTH DOMAIN IN YTH DOMAIN-2 CONTAINING PROTEIN 2 | ||||||
Components | YTH domain containing protein 2 (YTHDC2) | ||||||
Keywords | RNA BINDING PROTEIN / MEIOSIS RELATED PROTEIN / Structural Genomics / PSI-2 / Protein Structure Initiative / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information germline cell cycle switching, mitotic to meiotic cell cycle / ribonucleoprotein granule / positive regulation by host of viral genome replication / 3'-5' RNA helicase activity / N6-methyladenosine-containing RNA reader activity / oocyte development / ATP-dependent activity, acting on RNA / RNA polymerase binding / spermatid development / response to tumor necrosis factor ...germline cell cycle switching, mitotic to meiotic cell cycle / ribonucleoprotein granule / positive regulation by host of viral genome replication / 3'-5' RNA helicase activity / N6-methyladenosine-containing RNA reader activity / oocyte development / ATP-dependent activity, acting on RNA / RNA polymerase binding / spermatid development / response to tumor necrosis factor / response to interleukin-1 / meiotic cell cycle / helicase activity / RNA helicase / perinuclear region of cytoplasm / endoplasmic reticulum / ATP hydrolysis activity / RNA binding / ATP binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Muto, Y. / Kobayashi, N. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: TO BE PUBLISHED Title: SOLUTION STRUCTURE OF THE YTH DOMAIN IN YTH DOMAIN-CONTAINING PROTEIN 2 Authors: Endo, R. / He, F. / Inoue, M. / Muto, Y. / Kigawa, T. / Shirouzu, M. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6lr2.cif.gz | 869.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6lr2.ent.gz | 729.3 KB | Display | PDB format |
PDBx/mmJSON format | 6lr2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6lr2_validation.pdf.gz | 464.8 KB | Display | wwPDB validaton report |
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Full document | 6lr2_full_validation.pdf.gz | 571.3 KB | Display | |
Data in XML | 6lr2_validation.xml.gz | 41 KB | Display | |
Data in CIF | 6lr2_validation.cif.gz | 72.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lr/6lr2 ftp://data.pdbj.org/pub/pdb/validation_reports/lr/6lr2 | 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: 16138.065 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: P060508-16 Production host: Cell-free gateway cloning vector N-term 8xHis eGFP pCellFree_G03 (others) References: UniProt: Q6ZMY0, UniProt: Q9H6S0*PLUS |
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Sequence details | Authors state that 6L2R has a mutation, L129Q based rs1132529 in dbSNP database. |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Sample state: isotropic / Type: 3D 13C,15N-SEPARATED NOESY SPECTRA |
-Sample preparation
Details | Type: solution Contents: 1.0 mg/mL [U-99% 13C; U-99% 15N] helicase, 90% H2O/10% D2O Details: 1mM D-DTT;0.02% NaN3 were used to keep the protein condition Label: 13C, 15N_sample / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1.0 mg/mL / Component: helicase / Isotopic labeling: [U-99% 13C; U-99% 15N] |
Sample conditions | Details: 20mM D-Tris-HCL (PH7.0); 100mM NaCl; 1mM D-DTT;0.02% NaN3 Ionic strength: 100 mM / Label: condition_1 / pH: 7 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: the structures are based on 3191 NOE-derived distance contrrains, 71 main chain dihedral angle constraints based on TALOS program and 51 side chain dihedral constraints based on NOE pattern. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with favorable non-bond energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |