[English] 日本語
Yorodumi
- PDB-6prv: 58nt RNA L11-binding domain from E. coli 23S rRNA -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6prv
Title58nt RNA L11-binding domain from E. coli 23S rRNA
Components23S rRNA23S ribosomal RNA
KeywordsRNA / ribosome / 23S rRNA
Function / homology: / RNA / RNA (> 10)
Function and homology information
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.71 Å
AuthorsConn, G.L. / Dunstan, M.S.
CitationJournal: J.Mol.Biol. / Year: 2020
Title: Ribosomal Protein L11 Selectively Stabilizes a Tertiary Structure of the GTPase Center rRNA Domain.
Authors: Welty, R. / Rau, M. / Pabit, S. / Dunstan, M.S. / Conn, G.L. / Pollack, L. / Hall, K.B.
History
DepositionJul 11, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 8, 2020Provider: repository / Type: Initial release
Revision 1.1Mar 11, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation.year
Revision 1.2Oct 11, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: 23S rRNA
B: 23S rRNA
C: 23S rRNA
D: 23S rRNA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,10029
Polymers75,4484
Non-polymers65225
Water362
1
A: 23S rRNA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)19,12011
Polymers18,8621
Non-polymers25810
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: 23S rRNA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)19,0237
Polymers18,8621
Non-polymers1616
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: 23S rRNA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)19,0478
Polymers18,8621
Non-polymers1857
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: 23S rRNA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,9113
Polymers18,8621
Non-polymers492
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)89.610, 73.610, 130.280
Angle α, β, γ (deg.)90.000, 100.961, 90.000
Int Tables number5
Space group name H-MC121
Space group name HallC2y
Symmetry operation#1: x,y,z
#2: -x,y,-z
#3: x+1/2,y+1/2,z
#4: -x+1/2,y+1/2,-z
Components on special symmetry positions
IDModelComponents
11A-1207-

MG

-
Components

#1: RNA chain
23S rRNA / 23S ribosomal RNA


Mass: 18862.111 Da / Num. of mol.: 4 / Fragment: 58nt RNA L11-binding domain / Source method: obtained synthetically / Source: (synth.) Escherichia coli (E. coli)
#2: Chemical...
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 22 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: K / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.8 Å3/Da / Density % sol: 56 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 5-20 % PEG 4000, 0.6-1.2M NaCl and Sodium cacodylate (PH6.5)

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.97625 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 17, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 2.71→40 Å / Num. obs: 22407 / % possible obs: 97.9 % / Redundancy: 5.1 % / Biso Wilson estimate: 82.94 Å2 / CC1/2: 0.99 / Rrim(I) all: 0.086 / Net I/σ(I): 12.92
Reflection shellResolution: 2.71→2.87 Å / Mean I/σ(I) obs: 4.9 / Num. unique obs: 3442 / CC1/2: 0.49 / Rrim(I) all: 2.36

-
Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
PHENIX1.15.2_3472refinement
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1HC8
Resolution: 2.71→39.36 Å / SU ML: 0.4274 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 34.9446
RfactorNum. reflection% reflection
Rfree0.26 1110 4.99 %
Rwork0.2039 --
obs0.2067 22223 96.88 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 108.38 Å2
Refinement stepCycle: LAST / Resolution: 2.71→39.36 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms0 5000 25 2 5027
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0055588
X-RAY DIFFRACTIONf_angle_d1.14098704
X-RAY DIFFRACTIONf_chiral_restr0.04981156
X-RAY DIFFRACTIONf_plane_restr0.0071232
X-RAY DIFFRACTIONf_dihedral_angle_d16.05922780
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.71-2.830.49191270.4092413X-RAY DIFFRACTION88.94
2.83-2.980.41390.29992628X-RAY DIFFRACTION97.7
2.98-3.160.30511380.26112644X-RAY DIFFRACTION97.68
3.16-3.410.2941390.22442649X-RAY DIFFRACTION96.84
3.41-3.750.29911400.20292655X-RAY DIFFRACTION98.35
3.75-4.290.25471400.18412672X-RAY DIFFRACTION98.42
4.29-5.410.23761430.18012720X-RAY DIFFRACTION99.27
5.41-39.360.21471440.18882732X-RAY DIFFRACTION97.79
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)
10.125806836098-0.07123490350650.08261288017080.158988057878-0.1630532446430.106753456647-0.08769390415970.1741109480290.2133641797350.003570990303710.0917904944791-0.01362669060080.3615532080060.0254349614383-3.31910878836E-50.642288569577-0.0134445095868-0.0346061871550.6590646491940.02782056755720.76030284248624.87037568554.15508841223-10.0135301336
20.05658708891470.0266841539826-0.1060290333290.155385113308-0.09734366643590.18134024260.08064386467480.646547228230.325401459528-0.09309845035860.0062703488005-0.1823188480930.367344799775-0.385046306795-0.0002115724418420.826397879195-0.1344881496640.0476148929971.026468410940.1773838784290.820705790260.687183332492-3.7591010588-27.42610382
30.2238286134010.133956399670.1033404340470.1075047570960.12793477660.144357473222-0.3952732010860.3566137772060.205905654498-0.0771365576146-0.102606692051-0.1458565095740.820913234949-0.105855141935-0.0003720235727781.06098086844-0.1477004854870.06169241155790.9276970317290.1682608501820.76503675455415.782789342131.3035942329-27.7201368895
40.04905637346220.023497152962-0.1261485901930.0683974931844-0.02792560349440.41806610303-0.05112537344410.0009581660101340.000148171284049-0.0635726973054-0.4603496918130.454864411750.0143009685545-0.280054553397-0.9234251498651.45388457440.4832042235350.1569313297622.3261096051-1.30431239471.4463514215635.31993746829.0301323634-60.4342928908
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain 'A' and resid 1051 through 1108)
2X-RAY DIFFRACTION2(chain 'B' and resid 1051 through 1108)
3X-RAY DIFFRACTION3(chain 'C' and resid 1051 through 1108)
4X-RAY DIFFRACTION4(chain 'D' and resid 1051 through 1108)

+
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