2RA2

X-Ray structure of the Q7CPV8 protein from Salmonella typhimurium at the resolution 1.9 A. Northeast Structural Genomics Consortium target StR88A

PDB DOI: https://doi.org/10.2210/pdb2RA2/pdb

Classification: LIPOPROTEIN
Organism(s): Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2007-09-14 Released: 2007-10-09
Deposition Author(s): Kuzin, A.P., Su, M., Seetharaman, J., Vorobiev, S.M., Wang, H., Mao, L., Cunningham, K., Xiao, R., Liu, J., Baran, M.C., 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: 1.90 Å
R-Value Free: 0.251
R-Value Work: 0.228
R-Value Observed: 0.228

wwPDB Validation 3D Report Full Report

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

Literature

X-Ray structure of the Q7CPV8 protein from Salmonella typhimurium at the resolution 1.9 A.

Kuzin, A.P., Su, M., Seetharaman, J., Vorobiev, S.M., Wang, H., Mao, L., Cunningham, K., Xiao, R., Liu, J., Baran, M.C., Acton, T.B., Rost, B., Montelione, G.T., Hunt, J.F., Tong, L.

To be published.

Macromolecule Content

Total Structure Weight: 44.8 kDa
Atom Count: 2,788
Modelled Residue Count: 330
Deposited Residue Count: 384
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Putative lipoprotein	A, B, C, D, E A, B, C, D, E, F	64	Salmonella enterica subsp. enterica serovar Typhimurium str. LT2	Mutation(s): 0 Gene Names: ygdI, STM2983
UniProt
Find proteins for Q7CPV8 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)) Explore Q7CPV8 Go to UniProtKB: Q7CPV8
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q7CPV8
Sequence Annotations Expand
Reference Sequence

Small Molecules

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

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.251
R-Value Work: 0.228
R-Value Observed: 0.228
Space Group: C 2 2 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 68.292	α = 90
b = 110.426	β = 90
c = 109.02	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
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: 2007-10-09

Deposition Author(s):

Seetharaman, J.

Montelione, G.T.

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2007-10-09
Type: Initial release
Version 1.1: 2011-07-13
Changes: 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.