2HRX

X-Ray Crystal Structure of Protein DIP2367 from Corynebacterium diphtheriae. Northeast Structural Genomics Consortium Target CdR13.

PDB DOI: https://doi.org/10.2210/pdb2HRX/pdb

Classification: STRUCTURAL GENOMICS, UNKNOWN FUNCTION
Organism(s): Corynebacterium diphtheriae
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2006-07-20 Released: 2006-08-22
Deposition Author(s): Kuzin, A.P., Su, M., Jayaraman, S., Ho, C.K., Janjua, H., Cunningham, K., Ma, L.C., Xiao, R., Liu, J., Baran, M., Acton, T.B., Rost, B., Montelione, G.T., Tong, L., Hunt, J.F., Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.222
R-Value Work: 0.193
R-Value Observed: 0.193

wwPDB Validation 3D Report Full Report

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

Literature

Three dimensional structure of conserved hypothetical protein from Corynebacterium diphtheriae at the resolution 1.9 A. Northeast Structural Genomics Consortium target CdR13.

Kuzin, A.P., Su, M., Jayaraman, S., Ho, C.K., Janjua, H., Cunningham, K., Ma, L.C., Xiao, R., Liu, J., Baran, M., Acton, T.B., Rost, B., Montelione, G.T., Tong, L., Hunt, J.F.

To be published.

Macromolecule Content

Total Structure Weight: 22.93 kDa
Atom Count: 1,606
Modelled Residue Count: 191
Deposited Residue Count: 207
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Hypothetical protein	A	207	Corynebacterium diphtheriae	Mutation(s): 8
UniProt
Find proteins for Q6NEA9 (Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)) Explore Q6NEA9 Go to UniProtKB: Q6NEA9
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q6NEA9
Sequence Annotations Expand
Reference Sequence

Small Molecules

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

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.222
R-Value Work: 0.193
R-Value Observed: 0.193
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 35.526	α = 90
b = 75.034	β = 95.91
c = 36.873	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
DENZO	data reduction
SCALEPACK	data scaling
SOLVE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2006-08-22

Deposition Author(s):

Montelione, G.T.

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2006-08-22
Type: Initial release
Version 1.1: 2008-05-01
Changes: Version format compliance
Version 1.2: 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.