1NE2

Crystal Structure of Thermoplasma acidophilum 1320 (APC5513)

PDB DOI: https://doi.org/10.2210/pdb1NE2/pdb

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

Deposited: 2002-12-10 Released: 2003-07-01
Deposition Author(s): Kim, Y., Joachimiak, A., Edwards, A., Xu, X., Christendat, D., Midwest Center for Structural Genomics (MCSG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.75 Å
R-Value Free: 0.236
R-Value Work: 0.209
R-Value Observed: 0.209

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Crystal Structure of Thermoplasma acidophilum 1320 (APC5513)

Kim, Y., Joachimiak, A., Edwards, A., Xu, X., Christendat, D.

To be published.

Macromolecule Content

Total Structure Weight: 45.41 kDa
Atom Count: 3,090
Modelled Residue Count: 360
Deposited Residue Count: 400
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 ta1320	A, B	200	Thermoplasma acidophilum	Mutation(s): 4 Gene Names: Ta1320
UniProt
Find proteins for Q9HIL9 (Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)) Explore Q9HIL9 Go to UniProtKB: Q9HIL9
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9HIL9
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FMT Query on FMT Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A]	C [auth A]	FORMIC ACID C H₂ O₂ BDAGIHXWWSANSR-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]

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: 1.75 Å
R-Value Free: 0.236
R-Value Work: 0.209
R-Value Observed: 0.209
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 48.086	α = 90
b = 53.359	β = 90
c = 149.807	γ = 90

Software Package:

Software Name	Purpose
d*TREK	data scaling
HKL-2000	data collection
HKL-2000	data reduction
autoSHARP	phasing
CNS	refinement
d*TREK	data reduction
HKL-2000	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2003-07-01

Deposition Author(s):

Christendat, D.

Midwest Center for Structural Genomics (MCSG)

Revision History (Full details and data files)

Version 1.0: 2003-07-01
Type: Initial release
Version 1.1: 2008-04-28
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2017-10-11
Changes: Refinement description

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.