5OUN

NMR solution structure of the external DII domain of Rvb2 from Saccharomyces cerevisiae

PDB DOI: https://doi.org/10.2210/pdb5OUN/pdb
BMRB: 34173

Classification: HYDROLASE
Organism(s): Saccharomyces cerevisiae
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2017-08-24 Released: 2018-03-28
Deposition Author(s): Rouillon, C., Bragantini, B., Charpentier, B., Manival, X., Quinternet, M.
Funding Organization(s): French National Research Agency

Experimental Data Snapshot

Method: SOLUTION NMR
Conformers Calculated: 100
Conformers Submitted: 20
Selection Criteria: structures with the lowest energy

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

NMR assignment and solution structure of the external DII domain of the yeast Rvb2 protein.

Bragantini, B., Rouillon, C., Charpentier, B., Manival, X., Quinternet, M.

(2018) Biomol NMR Assign 12: 243-247

PubMed: 29569106 Search on PubMed
DOI: https://doi.org/10.1007/s12104-018-9816-5
Primary Citation of Related Structures:
5OUN

PubMed Abstract:
We report the nearly complete ¹H, ¹⁵N and ¹³C resonance assignment and the solution structure of the external DII domain of the yeast Rvb2 protein, a member of the AAA+ATPase superfamily.

Organizational Affiliation

Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), UMR 7365 CNRS Université de Lorraine, Biopôle, Campus Biologie Santé, Vandœuvre-lès-Nancy, France.

Macromolecule Content

Total Structure Weight: 11.85 kDa
Atom Count: 826
Modelled Residue Count: 107
Deposited Residue Count: 107
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
RuvB-like protein 2	A	107	Saccharomyces cerevisiae	Mutation(s): 0 Gene Names: RVB2, TIH2, TIP49B, YPL235W, P1060 EC: 3.6.4.12
UniProt
Find proteins for Q12464 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore Q12464 Go to UniProtKB: Q12464
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q12464
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: SOLUTION NMR
Conformers Calculated: 100
Conformers Submitted: 20
Selection Criteria: structures with the lowest energy

Structure Validation

View Full Validation Report

Entry History & Funding Information

Deposition Data

Released Date: 2018-03-28

Deposition Author(s):

Funding Organization	Location	Grant Number
French National Research Agency	France	ANR-16-CE11-0032-02

Revision History (Full details and data files)

Version 1.0: 2018-03-28
Type: Initial release
Version 1.1: 2018-04-04
Changes: Data collection, Database references
Version 1.2: 2018-09-19
Changes: Data collection, Database references
Version 1.3: 2019-05-08
Changes: Data collection
Version 1.4: 2023-06-14
Changes: Data collection, Database references, Other