3F08

Crystal structure of the putative uncharacterized protein Q6HG14 from Bacilllus thuringiensis. Northeast Structural Genomics Consortium target BuR153.

PDB DOI: https://doi.org/10.2210/pdb3F08/pdb

Classification: structural genomics, unknown function
Organism(s): [Bacillus thuringiensis] serovar konkukian
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2008-10-24 Released: 2008-11-18
Deposition Author(s): Kuzin, A.P., Abashidze, M., Seetharaman, J., Wang, H., Mao, L., Ciccosanti, C., Xiao, R., Nair, R., Baran, M.C., Swapna, G.V.T., Acton, T.B., Rost, B., Montelione, G.T., Hunt, J.F., Tong, L., Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.20 Å
R-Value Free: 0.237
R-Value Work: 0.203
R-Value Observed: 0.203

wwPDB Validation 3D Report Full Report

This is version 1.5 of the entry. See complete history.

Literature

Crystal structure of the putative uncharacterized protein Q6HG14 from Bacilllus thuringiensis. Northeast Structural Genomics Consortium target BuR153.

Kuzin, A.P., Abashidze, M., Seetharaman, J., Wang, H., Mao, L., Ciccosanti, C., Xiao, R., Nair, R., Baran, M.C., Swapna, G.V.T., Acton, T.B., Rost, B., Montelione, G.T., Hunt, J.F., Tong, L.

To be published.

Macromolecule Content

Total Structure Weight: 33.34 kDa
Atom Count: 2,295
Modelled Residue Count: 275
Deposited Residue Count: 292
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 Q6HG14	A, B	146	[Bacillus thuringiensis] serovar konkukian	Mutation(s): 5 Gene Names: BT9727_3189
UniProt
Find proteins for Q6HG14 (Bacillus thuringiensis subsp. konkukian (strain 97-27)) Explore Q6HG14 Go to UniProtKB: Q6HG14
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q6HG14
Sequence Annotations Expand
Reference Sequence

Small Molecules

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: 2.20 Å
R-Value Free: 0.237
R-Value Work: 0.203
R-Value Observed: 0.203
Space Group: P 6₁ 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 129.666	α = 90
b = 129.666	β = 90
c = 75.432	γ = 120

Software Package:

Software Name	Purpose
ADSC	data collection
BALBES	phasing
CNS	refinement
HKL-2000	data reduction
SCALEPACK	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2008-11-18

Deposition Author(s):

Seetharaman, J.

Montelione, G.T.

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2008-11-18
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2011-11-16
Changes: Atomic model
Version 1.3: 2021-10-20
Changes: Database references, Derived calculations
Version 1.4: 2023-09-06
Changes: Data collection, Refinement description
Version 1.5: 2023-11-15
Changes: Data collection

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.