[English] 日本語
Yorodumi
- PDB-2m1a: HIV-1 Rev ARM peptide (residues T34-R50) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2m1a
TitleHIV-1 Rev ARM peptide (residues T34-R50)
ComponentsHIV-1 Rev arginine-rich motif (ARM)
KeywordsVIRAL PROTEIN / HIV / Rev / arginine-rich motif
Function / homologyAnti-repression trans-activator protein, REV protein / REV protein (anti-repression trans-activator protein) / host cell nucleolus / mRNA transport / host cell cytoplasm / DNA-binding transcription factor activity / RNA binding / Protein Rev
Function and homology information
Biological speciesHuman immunodeficiency virus 1
MethodSOLUTION NMR / torsion angle dynamics, TORSION ANGLE DYNAMICS
Model detailslowest energy, model 1
AuthorsCasu, F. / Duggan, B.M. / Hennig, M.
CitationJournal: Biophys.J. / Year: 2013
Title: The Arginine-Rich RNA-Binding Motif of HIV-1 Rev Is Intrinsically Disordered and Folds upon RRE Binding.
Authors: Casu, F. / Duggan, B.M. / Hennig, M.
History
DepositionNov 21, 2012Deposition site: BMRB / Processing site: RCSB
Revision 1.0Sep 11, 2013Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_spectrometer.model
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: HIV-1 Rev arginine-rich motif (ARM)


Theoretical massNumber of molelcules
Total (without water)3,2201
Polymers3,2201
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100target function
RepresentativeModel #1lowest energy

-
Components

#1: Protein/peptide HIV-1 Rev arginine-rich motif (ARM)


Mass: 3219.727 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus 1 / Description: Expression controlled with the T7 lac promoter / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / Variant (production host): DE3 / References: UniProt: G3C324*PLUS

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
Details: The data presented are for the Rev arginine-rich motif (ARM), which comprises native residues 34-50 of the HIV-1 Rev protein and constitutes the protein RNA-binding domain and nuclear import ...Details: The data presented are for the Rev arginine-rich motif (ARM), which comprises native residues 34-50 of the HIV-1 Rev protein and constitutes the protein RNA-binding domain and nuclear import signal. This NMR structure was solved in a 50% TFE/aqueous buffer mixture.
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1212D 1H-15N HSQC NH2 only
1322D 1H-13C HSQC
1423D HNCO
1523D HNCA
1623D HN(CO)CA
1723D CBCA(CO)NH
1823D HN(CA)CB
1923D HBHA(CO)NH
11023D H(CCO)NH
11113D 1H-15N NOESY
11223D 1H-13C NOESY
11323D (H)CCH-TOCSY
11413D HNHA

-
Sample preparation

Details
Solution-IDContentsSolvent system
11.0 mM [U-15N] Rev ARM peptide, 50 mM sodium phosphate, 150 mM potassium chloride, 1 mM EDTA, 1 mM DTT, 0.02 % sodium azide, 10.0 % [U-99% 2H] D2O, 40.0 % H2O, 50.0 % TFE, trifluoroethanol/watertrifluoroethanol/water
21.0 mM [U-13C; U-15N] Rev ARM peptide, 50 mM sodium phosphate, 150 mM potassium chloride, 1 mM EDTA, 1 mM DTT, 0.02 % sodium azide, 10.0 % [U-99% 2H] D2O, 40.0 % H2O, 50.0 % [U-99% 2H] TFE, trifluoroethanol/watertrifluoroethanol/water
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1.0 mMRev ARM peptide-1[U-15N]1
50 mMsodium phosphate-21
150 mMpotassium chloride-31
1 mMEDTA-41
1 mMDTT-51
0.02 %sodium azide-61
10.0 %D2O-7[U-99% 2H]1
40.0 %H2O-81
50.0 %TFE-91
1.0 mMRev ARM peptide-10[U-13C; U-15N]2
50 mMsodium phosphate-112
150 mMpotassium chloride-122
1 mMEDTA-132
1 mMDTT-142
0.02 %sodium azide-152
10.0 %D2O-16[U-99% 2H]2
40.0 %H2O-172
50.0 %TFE-18[U-99% 2H]2
Sample conditionspH: 7.4 / Temperature: 283 K

-
NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE8001
Bruker AvanceBrukerAVANCE7002
Bruker AvanceBrukerAVANCE6003

-
Processing

NMR software
NameVersionDeveloperClassification
CYANA2.1Guntert, Mumenthaler and Wuthrichstructure solution
TALOS+Cornilescu, Delaglio and Baxstructure solution
CYANAGuntert, Mumenthaler and Wuthrichrefinement
RefinementMethod: torsion angle dynamics, TORSION ANGLE DYNAMICS / Software ordinal: 1
NMR constraintsNOE constraints total: 236 / NOE intraresidue total count: 118 / NOE long range total count: 0 / NOE medium range total count: 53 / NOE sequential total count: 65 / Protein phi angle constraints total count: 24 / Protein psi angle constraints total count: 24
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

+
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://pdbjlvh1.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