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Yorodumi- PDB-2l08: Solution NMR Structure of Nonsense mRNA reducing factor 3A from H... -
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-Basic information
Entry | Database: PDB / ID: 2l08 | ||||||
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Title | Solution NMR Structure of Nonsense mRNA reducing factor 3A from H. Sapiens, Northeast Structural Genomics Consortium Target HR4714B | ||||||
Components | Regulator of nonsense transcripts 3A | ||||||
Keywords | TRANSPORT PROTEIN / NESG / Nonsense regulator / Structural Genomics / PSI-2 / Protein Structure Initiative / Northeast Structural Genomics Consortium | ||||||
Function / homology | Function and homology information negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / positive regulation of mRNA cis splicing, via spliceosome / exon-exon junction complex / telomeric DNA binding / mRNA transport / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / positive regulation of translation / Regulation of expression of SLITs and ROBOs / spermatogenesis / in utero embryonic development ...negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / positive regulation of mRNA cis splicing, via spliceosome / exon-exon junction complex / telomeric DNA binding / mRNA transport / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / positive regulation of translation / Regulation of expression of SLITs and ROBOs / spermatogenesis / in utero embryonic development / neuron projection / mRNA binding / intracellular membrane-bounded organelle / nucleolus / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Mani, R. / Mao, L. / Ciccosanti, C. / Shastry, R. / Acton, T.B. / Xiao, R. / Swapna, G.V.T. / Everett, J.K. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
Citation | Journal: To be Published Title: Solution NMR Structure of Nonsense mRNA reducing factor 3A from H. Sapiens, Northeast Structural Genomics Consortium Target HR4714B Authors: Mani, R. / Mao, L. / Ciccosanti, C. / Shastry, R. / Acton, T.B. / Xiao, R. / Swapna, G.V.T. / Everett, J.K. / Montelione, G.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l08.cif.gz | 694.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l08.ent.gz | 590.3 KB | Display | PDB format |
PDBx/mmJSON format | 2l08.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l0/2l08 ftp://data.pdbj.org/pub/pdb/validation_reports/l0/2l08 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11596.175 Da / Num. of mol.: 1 / Fragment: sequence database residues 70-155 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: UPF3A, RENT3A, UPF3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)+ magic / References: UniProt: Q9H1J1 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: HR4714B is a 97 residue protein consisiting of a 10 residue N-terminal tag. N-HSQC spectrum shows only 71 peaks out of the 87 peaks (excluding tag) that are expected. The line broeadening of ...Details: HR4714B is a 97 residue protein consisiting of a 10 residue N-terminal tag. N-HSQC spectrum shows only 71 peaks out of the 87 peaks (excluding tag) that are expected. The line broeadening of the peaks occur from residue D45 to S54. Also, M11, R16, S81 NH's are missing from N-HSQC spectrum. The reason for line broadening is not known. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The Structure was obtained using triple resonance NMR spectroscopy for backbone and side chain assignments. Automated NOESY assignments were made using Autostructure and CYANA3.0. Dihedral ...Text: The Structure was obtained using triple resonance NMR spectroscopy for backbone and side chain assignments. Automated NOESY assignments were made using Autostructure and CYANA3.0. Dihedral angle constraints were obtained using TALOS. The structure calculation was done excluding the 10-residue N-terminal tag. Completeness of assignment excluding the tag: Backbone - 80%, Sidechain - 80%. Peaks for 13 residues in NHSQC spectra are missing due to line broadening. |
-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 100mM NaCl, 10mM Tris-HCl / pH: 7.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: Final structure quality (excluding 10 residue tag) determined using PSVS-v1.4: Ordered residues are defines as: 10-19,22-34,36-45,54-72,76-94. (a) RMSD (ordered residues) all backbone aroms: ...Details: Final structure quality (excluding 10 residue tag) determined using PSVS-v1.4: Ordered residues are defines as: 10-19,22-34,36-45,54-72,76-94. (a) RMSD (ordered residues) all backbone aroms: 0.6A. and heavy atoms 1.0A. (b) Ramachandran statistics for ordered residues: Most favored region: 85.1% Additionally favored region: 14.8% Generaously allowed region: 0.1% Disallowed region: 0.1%. (c) Procheck scores for ordered residues (RAW/Z): Phi/psi -0.73/-2.56, all -0.65/-3.84, (d) Molprobity clashscores (RAW/Z)22.41/-2.32 (e) RPF scores for the goodness fit to NOESY data: Recall: 89, Precision: 94, F-measure: 92, final dp-score - (f) RMS deviation for bond angles - 6.15, RMS deviation for bond lengths 0.01A. | ||||||||||||||||||||
NMR constraints | NOE constraints total: 1729 / NOE intraresidue total count: 281 / NOE long range total count: 333 / NOE medium range total count: 536 / NOE sequential total count: 471 / Protein phi angle constraints total count: 108 / Protein psi angle constraints total count: 108 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0.25 Å / Maximum torsion angle constraint violation: 8.5 ° / Maximum upper distance constraint violation: 1.7 Å | ||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.01 Å |