4wsa

Crystal structure of Influenza B polymerase bound to the vRNA promoter (FluB1 form)

Method: X-RAY DIFFRACTION Dmax: 131.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

PA

Influenza B virus

UniProt Q5V8Z9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 3 RNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain A; UniProt 1–726 Not recorded ;Influenza B vRNA promoter 3' end ; × 1 ;Influenza B vRNA promoter 5' end ; × 1 RNA-directed RNA polymerase catalytic subunit × 1 (Q5V8Y6) PB2 × 1 (Q5V8X3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;281 K;FluB polymerase was concentrated to 9 mg per ml (37 microM) in a buffer containing 500 mM NaCl, 50 mM Hepes pH 7.5, 5% glycerol and 2mM Tris(2-carboxyethyl)phosphine (TCEP), and mixed with 40 microM vRNA for crystallization in hanging drops at 4 C. A trigonal crystal form (FluB1) was obtained by mixing polymerase with nucleotides 5-18 of the 3 prime end and 1-14 of the 5 prime end of the vRNA in a condition containing 0.1 M bicine pH 9.0, 10% MPD. Resolution 3.40 Å R-free 0.265

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

34 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5V8Z9_9INFB
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 15–740; UniProt 1–726

RNA-directed RNA polymerase catalytic subunit

Influenza B virus

UniProt Q5V8Y6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 3 RNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain B; UniProt 1–752 Mutation:Trichoplusia ni ;Influenza B vRNA promoter 3' end ; × 1 ;Influenza B vRNA promoter 5' end ; × 1 PA × 1 (Q5V8Z9) PB2 × 1 (Q5V8X3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;281 K;FluB polymerase was concentrated to 9 mg per ml (37 microM) in a buffer containing 500 mM NaCl, 50 mM Hepes pH 7.5, 5% glycerol and 2mM Tris(2-carboxyethyl)phosphine (TCEP), and mixed with 40 microM vRNA for crystallization in hanging drops at 4 C. A trigonal crystal form (FluB1) was obtained by mixing polymerase with nucleotides 5-18 of the 3 prime end and 1-14 of the 5 prime end of the vRNA in a condition containing 0.1 M bicine pH 9.0, 10% MPD. Resolution 3.40 Å R-free 0.265

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

30 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5V8Y6_9INFB
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 10–761; UniProt 1–752

PB2

Influenza B virus

UniProt Q5V8X3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 3 RNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain C; UniProt 1–770 Not recorded ;Influenza B vRNA promoter 3' end ; × 1 ;Influenza B vRNA promoter 5' end ; × 1 PA × 1 (Q5V8Z9) RNA-directed RNA polymerase catalytic subunit × 1 (Q5V8Y6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;281 K;FluB polymerase was concentrated to 9 mg per ml (37 microM) in a buffer containing 500 mM NaCl, 50 mM Hepes pH 7.5, 5% glycerol and 2mM Tris(2-carboxyethyl)phosphine (TCEP), and mixed with 40 microM vRNA for crystallization in hanging drops at 4 C. A trigonal crystal form (FluB1) was obtained by mixing polymerase with nucleotides 5-18 of the 3 prime end and 1-14 of the 5 prime end of the vRNA in a condition containing 0.1 M bicine pH 9.0, 10% MPD. Resolution 3.40 Å R-free 0.265

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

31 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5V8X3_9INFB
Isoform
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 10–779; UniProt 1–770

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 4wsa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4wsa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4wsa
Deposition date deposition_date2014-10-26
Structure title titleCrystal structure of Influenza B polymerase bound to the vRNA promoter (FluB1 form)
Keywords keywordsTRANSFERASE-RNA COMPLEX; TRANSFERASE/RNA
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier41.34
Radius of gyration Rg (electron density) rg_electron40.78
Forward intensity I(0) i01009370000.00
Molecular weight molecular_weight256480.0 kDa
Excluded volume excluded_volume319170 ų
Envelope volume envelope_volume429990 ų
Hydration-shell volume shell_volume83868 ų
Envelope diameter envelope_diameter134.3
Shell Rg shell_rg49.08
Envelope Rg envelope_rg40.44
Shape Rg shape_rg40.79
Total Rg total_rg41.14
Total atoms total_atoms17940
Residues n_residues2207
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax131.4
Rg (real space) rg_real41.15
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real1.0090e+09
I(0) uncertainty (real space) i0_real_error1.6930e+07
Rg (reciprocal space) rg_reciprocal41.34
I(0) (reciprocal space) i0_reciprocal1010000000.0000
Solution quality estimate total_estimate0.8841
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.9
Skewness Skewness skewness0.181
Kurtosis Kurtosis kurtosis-0.401
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha152200000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.882; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.873

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)