Helical symmetry: (Circular symmetry: 1 / Dyad axis: no / N subunits divisor: 1 / Num. of operations: 49 / Rise per n subunits: 1.439 Å / Rotation per n subunits: 22.041 °)
Details
HLSV IS A ROD-SHAPED VIRUS 3000 ANGSTROMS LONG AND 180 ANGSTROMS IN DIAMETER, WITH A CENTRAL HOLE OF DIAMETER 40 ANGSTROMS. APPROXIMATELY 2150 IDENTICAL PROTEIN SUBUNITS OF MOLECULAR WEIGHT 17500 FORM A RIGHT-HANDED HELIX OF PITCH 23.5 ANGSTROMS AND LENGTH 70.5 ANGTROMS WITH 49 SUBUNITS IN THREE TURNS. A SINGLE STRAND OF RNA FOLLOWS THE BASIC HELIX BETWEEN THE PROTEIN SUBUNITS AT A DISTANCE OF 40 ANGSTROMS. THERE ARE THREE NUCLEOTIDES BOUND TO EACH PROTEIN SUBUNIT. THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR HELICAL SYMMETRY WITH THE FOLLOWING PARAMETERS: ROTATION PER SUBUNIT (TWIST) = 1080.00/49 DEGREES RISE PER SUBUNIT (HEIGHT) = 70.5/49 ANGSTROMS COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
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Components
#1: RNA chain
RNA (5'-R(P*GP*AP*A)-3')
Mass: 958.660 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic RNA
#2: Protein
Coatprotein
Mass: 18079.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Hibiscus latent Singapore virus / References: UniProt: Q8BE68
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Experimental details
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Experiment
Experiment
Method: FIBER DIFFRACTION / Number of used crystals: 1
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.5→50 Å / σ(F): 1 / Stereochemistry target values: Engh & Huber Details: THE STRUCTURE WAS DETERMINED BY FIBER DIFFRACTION USING MOLECULAR REPLACEMENT WITH LAYER-LINE SPLITTING, SOLVENT FLATTENING REFINEMENT AND RESTRAINED LEAST SQUARES COORDINATE REFINEMENT. THE ...Details: THE STRUCTURE WAS DETERMINED BY FIBER DIFFRACTION USING MOLECULAR REPLACEMENT WITH LAYER-LINE SPLITTING, SOLVENT FLATTENING REFINEMENT AND RESTRAINED LEAST SQUARES COORDINATE REFINEMENT. THE STRUCTURE INCLUDES 162 OF THE 163 AMINO ACIDS AND THREE RNA NUCLEOTIDES MODELLED AS GAA BUT REPRESENTING THE ENTIRE NUCLEIC ACID CONTENT.
Rfactor
Num. reflection
Rwork
0.096
-
obs
0.096
3486
all
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3486
Refinement step
Cycle: LAST / Resolution: 3.5→50 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
1277
64
0
0
1341
+
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