2RA8

Crystal structure of the Q64V53_BACFR protein from Bacteroides fragilis. Northeast Structural Genomics Consortium target BfR43

PDB DOI: https://doi.org/10.2210/pdb2RA8/pdb

Classification: STRUCTURAL GENOMICS, UNKNOWN FUNCTION
Organism(s): Bacteroides fragilis YCH46
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2007-09-14 Released: 2007-09-25
Deposition Author(s): Vorobiev, S.M., Abashidze, M., Seetharaman, J., Wang, D., Cunningham, K., Maglaqui, M., Owens, L., Xiao, R., Acton, T.B., Montelione, G.T., Hunt, J.F., Tong, L., Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.95 Å
R-Value Free: 0.247
R-Value Work: 0.225
R-Value Observed: 0.225

wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Crystal structure of the Q64V53_BACFR protein from Bacteroides fragilis.

Vorobiev, S.M., Abashidze, M., Seetharaman, J., Wang, D., Cunningham, K., Maglaqui, M., Owens, L., Xiao, R., Acton, T.B., Montelione, G.T., Hunt, J.F., Tong, L.

To be published.

Macromolecule Content

Total Structure Weight: 41.85 kDa
Atom Count: 3,003
Modelled Residue Count: 351
Deposited Residue Count: 362
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 Q64V53_BACFR	A	362	Bacteroides fragilis YCH46	Mutation(s): 0 Gene Names: BF1877
UniProt
Find proteins for Q64V53 (Bacteroides fragilis (strain YCH46)) Explore Q64V53 Go to UniProtKB: Q64V53
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q64V53
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 2 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
CAS Query on CAS	A	L-PEPTIDE LINKING	C₅ H₁₂ As N O₂ S		CYS
MSE Query on MSE	A	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.95 Å
R-Value Free: 0.247
R-Value Work: 0.225
R-Value Observed: 0.225
Space Group: C 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 108.261	α = 90
b = 65.237	β = 111.13
c = 60.008	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
HKL-2000	data collection
DENZO	data reduction
SCALEPACK	data scaling
SOLVE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2007-09-25

Deposition Author(s):

Seetharaman, J.

Montelione, G.T.

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2007-09-25
Type: Initial release
Version 1.1: 2011-07-13
Changes: Source and taxonomy, Version format compliance

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.