5fml

Crystal structure of the endonuclease from the PA subunit of influenza B virus bound to the PB2 subunit NLS peptide

Method: X-RAY DIFFRACTION Dmax: 58.7 Å Quality: GOOD

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

PB2 SUBUNIT OF INFLUENZA B POLYMERASE

OrganismNot specified

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 742–770 Fragment:NLS PEPTIDE RESIDUES 742-770 PA SUBUNIT OF INFLUENZA B POLYMERASE × 1 (Q5V8Z9) MG MAGNESIUM ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.1 M MES PH 6.5, 25% PEG6000 Resolution 1.70 Å R-free 0.276

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–29; UniProt 742–770

PA SUBUNIT OF INFLUENZA B POLYMERASE

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–197 Fragment:ENDONUCLEASE DOMAIN RESIDUES 1-197 PB2 SUBUNIT OF INFLUENZA B POLYMERASE × 1 (Q5V8X3) MG MAGNESIUM ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;0.1 M MES PH 6.5, 25% PEG6000 Resolution 1.70 Å R-free 0.276

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 2
Chains and sequence ranges Author chain B; PDBConstruct 6–202; UniProt 1–197

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 5fml

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5fml
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5fml
Deposition date deposition_date2015-11-06
Structure title titleCrystal structure of the endonuclease from the PA subunit of influenza B virus bound to the PB2 subunit NLS peptide
Keywords keywordsVIRAL PROTEIN, ENDONUCLEASE; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.30
Radius of gyration Rg (electron density) rg_electron17.09
Forward intensity I(0) i011486100.00
Molecular weight molecular_weight24982.0 kDa
Excluded volume excluded_volume31222 ų
Envelope volume envelope_volume36147 ų
Hydration-shell volume shell_volume17559 ų
Envelope diameter envelope_diameter59.8
Shell Rg shell_rg23.33
Envelope Rg envelope_rg17.39
Shape Rg shape_rg17.09
Total Rg total_rg18.12
Total atoms total_atoms1749
Residues n_residues215
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 dmax58.7
Rg (real space) rg_real18.19
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real1.1490e+07
I(0) uncertainty (real space) i0_real_error1.2560e+05
Rg (reciprocal space) rg_reciprocal18.21
I(0) (reciprocal space) i0_reciprocal11490000.0000
Solution quality estimate total_estimate0.8854
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.358
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3141000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)