3USH

Crystal Structure of the Q2S0R5 protein from Salinibacter ruber, Northeast Structural Genomics Consortium Target SrR207

PDB DOI: https://doi.org/10.2210/pdb3USH/pdb

Classification: Structural Genomics, Unknown Function
Organism(s): Salinibacter ruber DSM 13855
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2011-11-23 Released: 2011-12-14
Deposition Author(s): Vorobiev, S., Su, M., Seetharaman, J., Maglaqui, M., Xiao, R., Kohan, E., Wang, D., Everett, J.K., Acton, T.B., Montelione, G.T., Tong, L., Hunt, J.F., Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.69 Å
R-Value Free: 0.194
R-Value Work: 0.171
R-Value Observed: 0.172

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Crystal Structure of the Q2S0R5 protein from Salinibacter ruber, Northeast Structural Genomics Consortium Target SrR207

Vorobiev, S., Su, M., Seetharaman, J., Maglaqui, M., Xiao, R., Kohan, E., Wang, D., Everett, J.K., Acton, T.B., Montelione, G.T., Tong, L., Hunt, J.F.

To be published.

Macromolecule Content

Total Structure Weight: 29.21 kDa
Atom Count: 1,983
Modelled Residue Count: 238
Deposited Residue Count: 258
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Uncharacterized protein	A, B	129	Salinibacter ruber DSM 13855	Mutation(s): 0 Gene Names: SRU_2110
UniProt
Find proteins for Q2S0R5 (Salinibacter ruber (strain DSM 13855 / M31)) Explore Q2S0R5 Go to UniProtKB: Q2S0R5
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q2S0R5
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
BR Query on BR Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth A] SDF format, chain E [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth A] MOL2 format, chain E [auth B]	C [auth A], D [auth A], E [auth B]	BROMIDE ION Br CPELXLSAUQHCOX-UHFFFAOYSA-M		Interactions Focus chain C [auth A] Focus chain D [auth A] Focus chain E [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth A] Focus chain E [auth B]

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A, B	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.69 Å
R-Value Free: 0.194
R-Value Work: 0.171
R-Value Observed: 0.172
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 31.079	α = 90
b = 85.417	β = 94.42
c = 42.8	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
PDB_EXTRACT	data extraction
ADSC	data collection
HKL-2000	data reduction
HKL-2000	data scaling
SnB	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2011-12-14

Deposition Author(s):

Seetharaman, J.

Montelione, G.T.

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2011-12-14
Type: Initial release
Version 1.1: 2017-11-08
Changes: Refinement description
Version 1.2: 2018-06-13
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.