[English] 日本語
Yorodumi
- PDB-2wac: Extended Tudor domain of Drosophila Melanogaster Tudor-SN (p100) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2wac
TitleExtended Tudor domain of Drosophila Melanogaster Tudor-SN (p100)
ComponentsCG7008-PA
KeywordsSPLICING / UNKNOWN FUNCTION / TUDOR / BETA-BARREL / NUCLEASE DOMAIN / TUDOR-SN / P100 / SND1 / METHYLATED ARGININE / SDMA
Function / homology
Function and homology information


: / nuclease activity / regulatory ncRNA-mediated gene silencing / RNA catabolic process / RISC complex / micrococcal nuclease / spermatogenesis / endonuclease activity / RNA binding / nucleus ...: / nuclease activity / regulatory ncRNA-mediated gene silencing / RNA catabolic process / RISC complex / micrococcal nuclease / spermatogenesis / endonuclease activity / RNA binding / nucleus / cytosol / cytoplasm
Similarity search - Function
RNA-induced silencing complex, nuclease component Tudor-SN / Tudor domain / Tudor domain profile. / Tudor domain / Tudor domain / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #90 / SH3 type barrels. - #140 / Staphylococcal nuclease (SNase-like), OB-fold / Staphylococcal nuclease homologue / Thermonuclease domain profile. ...RNA-induced silencing complex, nuclease component Tudor-SN / Tudor domain / Tudor domain profile. / Tudor domain / Tudor domain / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #90 / SH3 type barrels. - #140 / Staphylococcal nuclease (SNase-like), OB-fold / Staphylococcal nuclease homologue / Thermonuclease domain profile. / Staphylococcal nuclease homologues / SNase-like, OB-fold superfamily / SH3 type barrels. / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Roll / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Staphylococcal nuclease domain-containing protein 1
Similarity search - Component
Biological speciesDROSOPHILA MELANOGASTER (fruit fly)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsFriberg, A. / Corsini, L. / Sattler, M.
CitationJournal: J.Mol.Biol. / Year: 2009
Title: Structure and Ligand Binding of the Extended Tudor Domain of D. Melanogaster Tudor-Sn
Authors: Friberg, A. / Corsini, L. / Mourao, A. / Sattler, M.
History
DepositionFeb 4, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 3, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: CG7008-PA
B: CG7008-PA


Theoretical massNumber of molelcules
Total (without water)48,4672
Polymers48,4672
Non-polymers00
Water5,459303
1
A: CG7008-PA


Theoretical massNumber of molelcules
Total (without water)24,2331
Polymers24,2331
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: CG7008-PA


Theoretical massNumber of molelcules
Total (without water)24,2331
Polymers24,2331
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)83.560, 47.040, 129.770
Angle α, β, γ (deg.)90.00, 107.32, 90.00
Int Tables number5
Space group name H-MC121

-
Components

#1: Protein CG7008-PA / LD20211P / TUDOR-SN


Mass: 24233.254 Da / Num. of mol.: 2 / Fragment: TSN DOMAIN, TUDOR AND SN5, RESIDUES 700-916
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) DROSOPHILA MELANOGASTER (fruit fly) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: Q9W0S7
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 303 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.5 Å3/Da / Density % sol: 51 % / Description: NONE
Crystal growpH: 6.8 / Details: 20% PEG 3350, 100 MM BIS-TRIS PH 5.5, 200 MM NACL

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Wavelength: 1.54179
DetectorDate: Jun 2, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54179 Å / Relative weight: 1
ReflectionResolution: 2.1→19.64 Å / Num. obs: 28296 / % possible obs: 98.7 % / Observed criterion σ(I): 3 / Redundancy: 3.63 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 24.4
Reflection shellResolution: 2.1→2.22 Å / Redundancy: 3.51 % / Rmerge(I) obs: 0.15 / Mean I/σ(I) obs: 10.2 / % possible all: 97.8

-
Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2HQE
Resolution: 2.1→19.64 Å / Cor.coef. Fo:Fc: 0.925 / Cor.coef. Fo:Fc free: 0.893 / SU B: 11.159 / SU ML: 0.165 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.266 / ESU R Free: 0.212 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.269 1415 5 %RANDOM
Rwork0.227 ---
obs0.229 26881 98.7 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 25.08 Å2
Baniso -1Baniso -2Baniso -3
1-1.55 Å20 Å20.48 Å2
2---0.88 Å20 Å2
3----0.39 Å2
Refinement stepCycle: LAST / Resolution: 2.1→19.64 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3384 0 0 303 3687
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0223421
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.0371.9684647
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.7935433
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.70625.226155
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.03415577
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.7371518
X-RAY DIFFRACTIONr_chiral_restr0.0680.2536
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.022584
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1870.21304
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.290.22346
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1060.2261
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2160.256
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1250.216
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.3061.52233
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.3923470
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.46731353
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.784.51175
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.1→2.15 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.277 102 -
Rwork0.251 1945 -
obs--100 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
12.98920.1821-2.92620.9884-0.1565.0340.1118-0.19270.06030.0094-0.0301-0.1222-0.19220.5951-0.08170.00650.01770.0335-0.07060.0215-0.118626.138-25.9927.483
20.9380.446-1.68350.8817-0.60273.69190.01920.06830.0118-0.0926-0.01440.04610.0795-0.0247-0.0048-0.01660.0340.0447-0.14160.0075-0.180417.887-29.1167.024
32.2097-0.26120.19992.5642-0.53422.01120.0453-0.0196-0.07710.02130.02530.23750.0319-0.2636-0.07060.0024-0.00240.0633-0.14590.0142-0.1342-0.461-30.94724.006
47.08012.4494-0.58117.95520.22013.01510.0935-0.06610.1661-0.0825-0.05050.4403-0.1299-0.2223-0.04310.13560.00010.0775-0.11340.0182-0.1907-7.202-3.94446.343
50.5-0.75711.647611.5589-4.18415.7040.11520.0624-0.18892.3412-0.1339-0.0309-0.8481-0.14770.01870.9898-0.1050.1752-0.03340.0013-0.0683-4.001-3.61768.636
60.8766-0.0491-0.5193.5723-0.2613.50260.0612-0.0721-0.0840.1483-0.05740.23610.0238-0.059-0.00380.0612-0.01710.019-0.1590.0076-0.1077-2.03-7.0342.361
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A699 - 756
2X-RAY DIFFRACTION2A757 - 861
3X-RAY DIFFRACTION3A862 - 914
4X-RAY DIFFRACTION4B699 - 721
5X-RAY DIFFRACTION5B722 - 778
6X-RAY DIFFRACTION6B779 - 914

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more