[English] 日本語
Yorodumi
- PDB-1vk0: X-ray Structure of Gene Product from Arabidopsis Thaliana At5g06450 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1vk0
TitleX-ray Structure of Gene Product from Arabidopsis Thaliana At5g06450
Componentshypothetical protein
Keywordsstructural genomics / unknown function / Protein / homohexamer / Arabidopsis thaliana / At5g06450 / Protein Structure Initiative / Center for Eukaryotic Structural Genomics / CESG
Function / homology
Function and homology information


exoribonuclease II / exoribonuclease II activity / RISC complex binding / plant-type vacuole / single-stranded DNA 3'-5' DNA exonuclease activity / regulatory ncRNA-mediated gene silencing / positive regulation of miRNA metabolic process / : / nucleic acid binding / cytoplasm
Similarity search - Function
Ribonuclease H-like superfamily/Ribonuclease H / Nucleotidyltransferase; domain 5 / Ribonuclease H superfamily / Ribonuclease H-like superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Protein RISC-INTERACTING CLEARING 3'-5' EXORIBONUCLEASE 2
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.1 Å
AuthorsWesenberg, G.E. / Smith, D.W. / Phillips Jr., G.N. / Johnson, K.A. / Bingman, C.A. / Center for Eukaryotic Structural Genomics (CESG)
CitationJournal: To be published
Title: X-ray Structure of Gene Product from Arabidopsis Thaliana At5g06450
Authors: Center for Eukaryotic Structural Genomics
History
DepositionApr 12, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 27, 2004Provider: repository / Type: Initial release
Revision 1.1Feb 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Oct 4, 2017Group: Refinement description / Category: software
Revision 1.4Dec 27, 2023Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: hypothetical protein
B: hypothetical protein
C: hypothetical protein
D: hypothetical protein
E: hypothetical protein
F: hypothetical protein


Theoretical massNumber of molelcules
Total (without water)139,4586
Polymers139,4586
Non-polymers00
Water11,620645
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16780 Å2
ΔGint-79 kcal/mol
Surface area44900 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)120.831, 120.831, 185.222
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

-
Components

#1: Protein
hypothetical protein /


Mass: 23243.074 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: At5g06450 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9FNG3
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 645 / 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: 2.8 Å3/Da / Density % sol: 56.04 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8
Details: Sodium Citrate, Polyethylene glycol 2000, hepes, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 14-BM-D / Wavelength: 0.9792, 0.9800, 0.9641
DetectorType: MARRESEARCH / Detector: CCD / Date: Oct 26, 2003 / Details: Bent flat mirror and sagitally bent second crystal
RadiationMonochromator: Double crystal silicon 111 / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.97921
20.981
30.96411
ReflectionResolution: 2.1→35 Å / Num. obs: 91738 / % possible obs: 100 % / Redundancy: 10.6 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 29
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsDiffraction-ID% possible all
2.1-2.148.60.4795.8199.8
2.14-2.180.3671100
2.18-2.220.3321100
2.22-2.260.3251100
2.26-2.310.2641100
2.31-2.370.2451100
2.37-2.420.211100
2.42-2.490.1751100
2.49-2.560.1481100
2.56-2.650.1371100
2.65-2.740.1211100
2.74-2.850.11100
2.85-2.980.0851100
2.98-3.140.0671100
3.14-3.330.0521100
3.33-3.590.0421100
3.59-3.950.0361100
3.95-4.520.0311100
4.52-5.690.0321100
5.69-350.0311100

-
Phasing

PhasingMethod: MAD
Phasing set
ID
1
2
3
Phasing MADD res high: 3.5 Å / D res low: 20 Å / FOM : 0.78 / Reflection: 20131
Phasing MAD set
Clust-IDExpt-IDSet-IDWavelength (Å)F double prime refinedF prime refined
1110.97952.15-9.76
1120.97925.46-7.51
1130.96413.96-4.16
Phasing MAD set site
IDCartn x (Å)Cartn y (Å)Cartn z (Å)Atom type symbolB isoOccupancy
140.6418.7131.894SE48.40.36
235.24172.87728.131SE26.80.3
312.99347.1089.779SE450.34
4107.18610.2520.959SE39.90.35
53.14814.19426.837SE40.60.34
673.90716.66118.707SE39.10.31
Phasing MAD shell
Resolution (Å)FOM Reflection
11.16-200.871180
7.54-11.160.871732
6.04-7.540.852157
5.18-6.040.822480
4.61-5.180.82773
4.19-4.610.773016
3.87-4.190.723297
3.61-3.870.673496
Phasing dmFOM : 0.88 / FOM acentric: 0.89 / FOM centric: 0.79 / Reflection: 20132 / Reflection acentric: 17801 / Reflection centric: 2331
Phasing dm shell
Resolution (Å)FOM FOM acentricFOM centricReflectionReflection acentricReflection centric
10-19.990.970.970.92827603224
6.3-100.930.950.8527732313460
5-6.30.90.920.7833852964421
4.4-50.90.920.8134263058368
3.8-4.40.870.880.7660105454556
3.5-3.80.780.80.6137113409302

-
Processing

Software
NameVersionClassificationNB
SOLVE2.02phasing
RESOLVE2.02phasing
REFMACrefmac_5.1.24refinement
DENZOdata reduction
SCALEPACKdata scaling
PDB_EXTRACT1data extraction
RefinementMethod to determine structure: MAD / Resolution: 2.1→34.922 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.93 / SU B: 4.249 / SU ML: 0.114 / SU R Cruickshank DPI: 0.181 / Cross valid method: THROUGHOUT / ESU R: 0.181 / ESU R Free: 0.17
RfactorNum. reflection% reflectionSelection details
Rfree0.2326 4592 5.009 %RANDOM
Rwork0.1803 ---
all0.183 ---
obs0.1829 87085 99.98 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK
Displacement parametersBiso mean: 30.501 Å2
Baniso -1Baniso -2Baniso -3
1--0.008 Å2-0.004 Å20 Å2
2---0.008 Å20 Å2
3---0.011 Å2
Refinement stepCycle: LAST / Resolution: 2.1→34.922 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9546 0 0 645 10191
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0230.0219770
X-RAY DIFFRACTIONr_angle_refined_deg1.7771.94813236
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.71651188
X-RAY DIFFRACTIONr_chiral_restr0.1380.21491
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.027346
X-RAY DIFFRACTIONr_nbd_refined0.210.24278
X-RAY DIFFRACTIONr_nbtor_refined0.3170.26709
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1410.2653
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2050.236
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1710.212
X-RAY DIFFRACTIONr_mcbond_it1.98225943
X-RAY DIFFRACTIONr_mcangle_it3.56949555
X-RAY DIFFRACTIONr_scbond_it5.82663827
X-RAY DIFFRACTIONr_scangle_it8.02983681
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.1-2.15440.3033160.2356377670399.85
2.154-2.21320.2823340.261866520
2.213-2.27710.2752990.20460386337
2.277-2.34680.2733310.258276158
2.347-2.42350.2672960.19556865982
2.423-2.50810.2522900.18454785768
2.508-2.60220.2472870.17853335620
2.602-2.70790.2942710.18951145385
2.708-2.82750.2372340.17749655199
2.828-2.96450.2432520.18346784930
2.965-3.12370.2442430.19144884731
3.124-3.31150.2382310.18542644495
3.311-3.53780.2152140.17640124227
3.538-3.8180.2351940.1837433939
3.818-4.17750.1811850.14634803665
4.177-4.66220.1611890.14231113300
4.662-5.36750.2021370.15628092946
5.368-6.53540.2751240.19324092534
6.535-9.08470.2111010.18619042005
9.085-34.92150.207640.21211831247

+
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