5wme

Crystal Structure of Amino Acids 1729-1786 of Human Beta Cardiac Myosin Fused to Gp7 as Anti-Parallel Four-Helix Bundle

Method: X-RAY DIFFRACTION Dmax: 148.2 Å Quality: REASONABLE

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

Capsid assembly scaffolding protein,Myosin-7

Homo sapiens

UniProt P12883

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1728–1786 Chain B; UniProt 1728–1786 Chain C; UniProt 1728–1786 Chain D; UniProt 1728–1786 Fragment:UNP P13848 residues 2-48, UNP P12883 residues 1729-1786 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;298 K;18% (w/v) pentaerythritol ethoxylate 797, 150 mM ammonium thiocyanate, 100 mM sodium acetate pH 5.0. Resolution 2.30 Å R-free 0.264

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.

40 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYH7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 51–109; UniProt 1728–1786 Author chain B; PDBConstruct 51–109; UniProt 1728–1786 Author chain C; PDBConstruct 51–109; UniProt 1728–1786 Author chain D; PDBConstruct 51–109; UniProt 1728–1786

Capsid assembly scaffolding protein,Myosin-7

Homo sapiens

UniProt P13848

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–47 Chain B; UniProt 2–47 Chain C; UniProt 2–47 Chain D; UniProt 2–47 Fragment:UNP P13848 residues 2-48, UNP P12883 residues 1729-1786 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;298 K;18% (w/v) pentaerythritol ethoxylate 797, 150 mM ammonium thiocyanate, 100 mM sodium acetate pH 5.0. Resolution 2.30 Å R-free 0.264

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.

13 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SCAF_BPPH2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–50; UniProt 2–47 Author chain B; PDBConstruct 5–50; UniProt 2–47 Author chain C; PDBConstruct 5–50; UniProt 2–47 Author chain D; PDBConstruct 5–50; UniProt 2–47

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 5wme

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5wme
Deposition date deposition_date2017-07-28
Structure title titleCrystal Structure of Amino Acids 1729-1786 of Human Beta Cardiac Myosin Fused to Gp7 as Anti-Parallel Four-Helix Bundle
Keywords keywordsMyosin, Gp7, Coiled-Coil, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.99
Radius of gyration Rg (electron density) rg_electron43.04
Forward intensity I(0) i030119900.00
Molecular weight molecular_weight41558.0 kDa
Excluded volume excluded_volume51250 ų
Envelope volume envelope_volume70592 ų
Hydration-shell volume shell_volume18572 ų
Envelope diameter envelope_diameter156.3
Shell Rg shell_rg33.88
Envelope Rg envelope_rg43.80
Shape Rg shape_rg43.17
Total Rg total_rg42.01
Total atoms total_atoms2906
Residues n_residues365
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 dmax148.2
Rg (real space) rg_real42.07
Rg uncertainty (real space) rg_real_error2.51
I(0) (real space) i0_real3.0120e+07
I(0) uncertainty (real space) i0_real_error6.0240e+05
Rg (reciprocal space) rg_reciprocal41.00
I(0) (reciprocal space) i0_reciprocal30090000.0000
Solution quality estimate total_estimate0.5639
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.0
Skewness Skewness skewness0.721
Kurtosis Kurtosis kurtosis-0.283
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha759800.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.051; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.008; Smooth: 0.169

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)