4xa6

Crystal Structure of the coiled-coil surrounding Skip 4 of MYH7

Method: X-RAY DIFFRACTION Dmax: 207.0 Å Quality: REASONABLE

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

Gp7-MYH7(1777-1855)-EB1 chimera protein

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1777–1855 Chain B; UniProt 1777–1855 Fragment:UNP P13848 residues 2-50,UNP P02564 residues 1777-1855,UNP Q15691 residues 209-251 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;18% (w/v) polyethylene glycol 2000 methyl ether, 100 mM piperazine-N,N-bis(2-ethanesulfonic acid) (PIPES) Resolution 3.42 Å R-free 0.297
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1777–1855 Chain D; UniProt 1777–1855 Fragment:UNP P13848 residues 2-50,UNP P02564 residues 1777-1855,UNP Q15691 residues 209-251 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;18% (w/v) polyethylene glycol 2000 methyl ether, 100 mM piperazine-N,N-bis(2-ethanesulfonic acid) (PIPES) Resolution 3.42 Å R-free 0.297

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 54 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 54–132; UniProt 1777–1855 Author chain B; PDBConstruct 54–132; UniProt 1777–1855 Author chain C; PDBConstruct 54–132; UniProt 1777–1855 Author chain D; PDBConstruct 54–132; UniProt 1777–1855

Gp7-MYH7(1777-1855)-EB1 chimera protein

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–50 Chain B; UniProt 2–50 Fragment:UNP P13848 residues 2-50,UNP P02564 residues 1777-1855,UNP Q15691 residues 209-251 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;18% (w/v) polyethylene glycol 2000 methyl ether, 100 mM piperazine-N,N-bis(2-ethanesulfonic acid) (PIPES) Resolution 3.42 Å R-free 0.297
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2–50 Chain D; UniProt 2–50 Fragment:UNP P13848 residues 2-50,UNP P02564 residues 1777-1855,UNP Q15691 residues 209-251 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;18% (w/v) polyethylene glycol 2000 methyl ether, 100 mM piperazine-N,N-bis(2-ethanesulfonic acid) (PIPES) Resolution 3.42 Å R-free 0.297

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VG7_BPPH2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–53; UniProt 2–50 Author chain B; PDBConstruct 5–53; UniProt 2–50 Author chain C; PDBConstruct 5–53; UniProt 2–50 Author chain D; PDBConstruct 5–53; UniProt 2–50

Gp7-MYH7(1777-1855)-EB1 chimera protein

Homo sapiens

UniProt Q15691

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 209–251 Chain B; UniProt 209–251 Fragment:UNP P13848 residues 2-50,UNP P02564 residues 1777-1855,UNP Q15691 residues 209-251 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;18% (w/v) polyethylene glycol 2000 methyl ether, 100 mM piperazine-N,N-bis(2-ethanesulfonic acid) (PIPES) Resolution 3.42 Å R-free 0.297
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 209–251 Chain D; UniProt 209–251 Fragment:UNP P13848 residues 2-50,UNP P02564 residues 1777-1855,UNP Q15691 residues 209-251 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;298 K;18% (w/v) polyethylene glycol 2000 methyl ether, 100 mM piperazine-N,N-bis(2-ethanesulfonic acid) (PIPES) Resolution 3.42 Å R-free 0.297

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 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MARE1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 133–175; UniProt 209–251 Author chain B; PDBConstruct 133–175; UniProt 209–251 Author chain C; PDBConstruct 133–175; UniProt 209–251 Author chain D; PDBConstruct 133–175; UniProt 209–251

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 4xa6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4xa6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4xa6
Deposition date deposition_date2014-12-12
Structure title titleCrystal Structure of the coiled-coil surrounding Skip 4 of MYH7
Keywords keywordsMyosin, coiled coil, skip residue, fusion, Gp7, EB1, MYH7, Cardiac, 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_guinier53.01
Radius of gyration Rg (electron density) rg_electron54.70
Forward intensity I(0) i070956300.00
Molecular weight molecular_weight67756.0 kDa
Excluded volume excluded_volume84637 ų
Envelope volume envelope_volume141310 ų
Hydration-shell volume shell_volume26890 ų
Envelope diameter envelope_diameter200.6
Shell Rg shell_rg42.91
Envelope Rg envelope_rg53.80
Shape Rg shape_rg54.75
Total Rg total_rg53.95
Total atoms total_atoms4726
Residues n_residues488
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 dmax207.0
Rg (real space) rg_real54.08
Rg uncertainty (real space) rg_real_error3.99
I(0) (real space) i0_real7.0960e+07
I(0) uncertainty (real space) i0_real_error1.7010e+06
Rg (reciprocal space) rg_reciprocal52.12
I(0) (reciprocal space) i0_reciprocal70760000.0000
Solution quality estimate total_estimate0.6322
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.5
Skewness Skewness skewness0.653
Kurtosis Kurtosis kurtosis-0.358
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3254000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.172; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.112; Smooth: 0.588

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)