[English] 日本語
Yorodumi
- PDB-2k3b: Seeing the Invisible: Structures of Excited Protein States by Rel... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2k3b
TitleSeeing the Invisible: Structures of Excited Protein States by Relaxation Dispersion NMR
ComponentsActin-binding protein
KeywordsSTRUCTURAL PROTEIN / CPMG / Abp1p / Ark1p / Invisible State / Acetylation / Actin-binding / Cytoplasm / Cytoskeleton / Phosphoprotein / SH3 domain
Function / homology
Function and homology information


protein localization to actin cortical patch / positive regulation of Arp2/3 complex-mediated actin nucleation / actin cortical patch assembly / site of polarized growth / actin cortical patch / regulation of actin filament polymerization / mating projection tip / barbed-end actin filament capping / cortical actin cytoskeleton / actin filament binding ...protein localization to actin cortical patch / positive regulation of Arp2/3 complex-mediated actin nucleation / actin cortical patch assembly / site of polarized growth / actin cortical patch / regulation of actin filament polymerization / mating projection tip / barbed-end actin filament capping / cortical actin cytoskeleton / actin filament binding / cell cortex / cytoplasm
Similarity search - Function
Fungal actin-binding protein 1, second SH3 domain / Actin-depolymerising factor homology domain / Cofilin/tropomyosin-type actin-binding protein / ADF-H domain profile. / Actin depolymerisation factor/cofilin -like domains / ADF-H/Gelsolin-like domain superfamily / SH3 Domains / SH3 domain / SH3 type barrels. / Src homology 3 domains ...Fungal actin-binding protein 1, second SH3 domain / Actin-depolymerising factor homology domain / Cofilin/tropomyosin-type actin-binding protein / ADF-H domain profile. / Actin depolymerisation factor/cofilin -like domains / ADF-H/Gelsolin-like domain superfamily / SH3 Domains / SH3 domain / SH3 type barrels. / Src homology 3 domains / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Roll / Mainly Beta
Similarity search - Domain/homology
Actin-binding protein
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodSOLUTION NMR / simulated annealing
AuthorsVallurupalli, P. / Hansen, F.D. / Kay, L.E.
CitationJournal: Proc.Natl.Acad.Sci.Usa / Year: 2008
Title: Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy
Authors: Vallurupalli, P. / Hansen, D.F. / Kay, L.E.
History
DepositionApr 30, 2008Deposition site: BMRB / Processing site: RCSB
Revision 1.0Jul 29, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.3May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Actin-binding protein


Theoretical massNumber of molelcules
Total (without water)6,9931
Polymers6,9931
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)10 / 960structures with the lowest energy
RepresentativeModel #1lowest energy

-
Components

#1: Protein Actin-binding protein


Mass: 6993.485 Da / Num. of mol.: 1 / Fragment: SH3 domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: ABP1 / Production host: Escherichia coli (E. coli) / References: UniProt: P15891

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11115N CT-CW,TROSY,anti-TROSY CPMG
12215N CT-CW,TROSY,anti-TROSY CPMG
13313CO CT-inphase,TROSY,anti-TROSY CPMG
14413CA CT-CW,TROSY,anti-TROSY CPMG

-
Sample preparation

Details
Solution-IDContentsSolvent system
1~1.5 mM [90 % U 2H; ~100% U 15N] Abp1p, ~0.105 mM [90% U 2H; ~100% U 15N] Ark1p, 90% H2O/10% D2O90% H2O/10% D2O
2~1.5 mM [90 % U 2H; ~100% U 15N] Abp1p, ~0.105 mM Ark1p, 90% H2O/10% D2O90% H2O/10% D2O
3~1.5 mM [90 % U 2H; ~100% U 15N; 13CO labeled] Abp1p, ~0.105 mM Ark1p, 90% H2O/10% D2O90% H2O/10% D2O
4~1.5 mM [90 % U 2H; ~100% U 15N; 13Ca labeled] Abp1p, ~0.105 mM Ark1p, 100% D2O100% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1.5 mMAbp1p[90 % U 2H; ~100% U 15N]1
0.105 mMArk1p[90% U 2H; ~100% U 15N]1
1.5 mMAbp1p[90 % U 2H; ~100% U 15N]2
0.105 mMArk1p2
1.5 mMAbp1p[90 % U 2H; ~100% U 15N; 13CO labeled]3
0.105 mMArk1p3
1.5 mMAbp1p[90 % U 2H; ~100% U 15N; 13Ca labeled]4
0.105 mMArk1p4
Sample conditionsIonic strength: ~0.150 / pH: 7.0 / Pressure: ambient / Temperature: 278 K

-
NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA5001
Varian INOVAVarianINOVA8002
Varian INOVAVarianINOVA6003

-
Processing

NMR software
NameVersionDeveloperClassification
X-PLOR NIH2.19Schwieters, Kuszewski, Tjandra and Clorestructure solution
X-PLOR NIH2.19Schwieters, Kuszewski, Tjandra and Clorerefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 960 / Conformers submitted total number: 10

+
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