[English] 日本語
Yorodumi
- PDB-1w94: Crystal Structure of Mil (Mth680), an archaeal Imp4-like protein -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1w94
TitleCrystal Structure of Mil (Mth680), an archaeal Imp4-like protein
ComponentsPROBABLE BRIX-DOMAIN RIBOSOMAL BIOGENESIS PROTEIN
KeywordsARCHAEAL IMP4-BRIX DOMAIN / IMP4 DOMAIN / BRIX DOMAIN / RNA-BINDING PROTEIN
Function / homology
Function and homology information


ribosome biogenesis
Similarity search - Function
Brix domain / Probable Brix domain-containing ribosomal biogenesis protein / Brix domain / Brix domain profile. / Brix / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Probable Brix domain-containing ribosomal biogenesis protein
Similarity search - Component
Biological speciesMETHANOTHERMOBACTER THERMAUTOTROPHICUS (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2 Å
AuthorsNg, C.L. / Antson, A.A. / Ortiz-Lombardia, M.
CitationJournal: Embo Rep. / Year: 2005
Title: Crystal Structure of Mil (Mth680): Internal Duplication and Similarity between the Imp4/Brix Domain and the Anticodon-Binding Domain of Class Iia Aminoacyl-tRNA Synthetases
Authors: Ng, C.L. / Waterman, D. / Koonin, E.V. / Antson, A.A. / Ortiz-Lombardia, M.
History
DepositionOct 6, 2004Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 19, 2005Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: PROBABLE BRIX-DOMAIN RIBOSOMAL BIOGENESIS PROTEIN
B: PROBABLE BRIX-DOMAIN RIBOSOMAL BIOGENESIS PROTEIN


Theoretical massNumber of molelcules
Total (without water)36,1832
Polymers36,1832
Non-polymers00
Water2,468137
1
A: PROBABLE BRIX-DOMAIN RIBOSOMAL BIOGENESIS PROTEIN


Theoretical massNumber of molelcules
Total (without water)18,0921
Polymers18,0921
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: PROBABLE BRIX-DOMAIN RIBOSOMAL BIOGENESIS PROTEIN


Theoretical massNumber of molelcules
Total (without water)18,0921
Polymers18,0921
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)33.673, 77.533, 60.965
Angle α, β, γ (deg.)90.00, 100.01, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein PROBABLE BRIX-DOMAIN RIBOSOMAL BIOGENESIS PROTEIN / MIL


Mass: 18091.615 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) METHANOTHERMOBACTER THERMAUTOTROPHICUS (archaea)
Strain: DELTA H / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: O26776
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 137 / Source method: isolated from a natural source / Formula: H2O
Compound detailsBRIX DOMAIN INVOLVED IN RIBOSOME BIOGENESIS.

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2 Å3/Da / Density % sol: 38 %
Crystal growpH: 7.5
Details: THE PROTEIN AT APPROX. 10 MG/ML WAS CRYSTALLIZED IN 20% PEG3350 AND 0.1 M HEPES 7.5, pH 7.50

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.97935, 0.9795, 0.976565
DetectorType: MARRESEARCH / Detector: CCD / Date: Jun 26, 2004
RadiationProtocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.979351
20.97951
30.9765651
ReflectionResolution: 2→47.46 Å / Num. obs: 20938 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 9.23
Reflection shellResolution: 2→2.02 Å / Redundancy: 3.87 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 1.47 / % possible all: 100

-
Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
MOSFLMdata reduction
SCALAdata scaling
SHELXphasing
RefinementMethod to determine structure: MAD / Resolution: 2→60.08 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.923 / SU B: 9.816 / SU ML: 0.136 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.208 / ESU R Free: 0.175 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.24 1074 5.1 %RANDOM
Rwork0.198 ---
obs0.2 19845 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 31.43 Å2
Baniso -1Baniso -2Baniso -3
1--0.67 Å20 Å2-0.27 Å2
2---0.24 Å20 Å2
3---0.82 Å2
Refinement stepCycle: LAST / Resolution: 2→60.08 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2423 0 0 137 2560
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0222470
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.4011.9713316
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.6575300
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.66321.121116
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.02315454
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.1851538
X-RAY DIFFRACTIONr_chiral_restr0.1180.2349
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.021868
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2220.21012
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3070.21675
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2150.2144
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1880.247
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.0860.28
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.1741.51554
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.35222417
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.4831037
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.7674.5899
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→2.05 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.325 87
Rwork0.27 1449
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)
11.95260.13340.35471.92230.28931.66460.0172-0.05370.0826-0.06-0.04340.14240.0214-0.10120.0261-0.1305-0.00580.0031-0.1360.0067-0.13883.0303-17.329-24.2262
24.05060.08751.15813.12240.39033.94810.0573-0.4739-0.50830.37020.0018-0.11930.2565-0.1909-0.0591-0.0326-0.0533-0.00920.01660.0851-0.061613.8334-26.59791.1769
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 154
2X-RAY DIFFRACTION2B1 - 154

+
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