1i84

CRYO-EM STRUCTURE OF THE HEAVY MEROMYOSIN SUBFRAGMENT OF CHICKEN GIZZARD SMOOTH MUSCLE MYOSIN WITH REGULATORY LIGHT CHAIN IN THE DEPHOSPHORYLATED STATE. ONLY C ALPHAS PROVIDED FOR REGULATORY LIGHT CHAIN. ONLY BACKBONE ATOMS PROVIDED FOR S2 FRAGMENT.

Method: ELECTRON CRYSTALLOGRAPHY Dmax: 172.8 Å Quality: GOOD

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

SMOOTH MUSCLE MYOSIN HEAVY CHAIN

Gallus gallus

UniProt P10587

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain S; UniProt 1–1174 Chain V; UniProt 1–1174 Fragment:MEROMYOSIN SUBFRAGMENT. S1 AND S2 FRAGMENTS. Non-standard monomer:Yes (specific site not provided by mmCIF) SMOOTH MUSCLE MYOSIN ESSENTIAL LIGHT CHAIN × 2 SMOOTH MUSCLE MYOSIN REGULATORY LIGHT CHAIN × 2 (P02609) ELECTRON CRYSTALLOGRAPHY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Specimens were frozen in liquid ethane using a drop freezing apparatus. X-ray crystallization conditions:Lipid monolayer;pH 7.5;277 K;MgCl, sodium phosphate, ATP, EGTA, PEG 6000, pH 7.5, Lipid monolayer, temperature 277K Resolution 20.00 Å

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.

8 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYSG_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain S; PDBConstruct 1–1174; UniProt 1–1174 Author chain V; PDBConstruct 1–1174; UniProt 1–1174

SMOOTH MUSCLE MYOSIN REGULATORY LIGHT CHAIN

Gallus gallus

UniProt P02609

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain U; UniProt 1–166 Chain Z; UniProt 1–166 Fragment:S1 FRAGMENT SMOOTH MUSCLE MYOSIN HEAVY CHAIN × 2 (P10587) SMOOTH MUSCLE MYOSIN ESSENTIAL LIGHT CHAIN × 2 ELECTRON CRYSTALLOGRAPHY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Specimens were frozen in liquid ethane using a drop freezing apparatus. X-ray crystallization conditions:Lipid monolayer;pH 7.5;277 K;MgCl, sodium phosphate, ATP, EGTA, PEG 6000, pH 7.5, Lipid monolayer, temperature 277K Resolution 20.00 Å

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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLRS_CHICK
Isoform
PDB entities 3
Chains and sequence ranges Author chain U; PDBConstruct 1–166; UniProt 1–166 Author chain Z; PDBConstruct 1–166; UniProt 1–166

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 1i84

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1i84
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1i84
Deposition date deposition_date2001-03-12
Structure title titleCRYO-EM STRUCTURE OF THE HEAVY MEROMYOSIN SUBFRAGMENT OF CHICKEN GIZZARD SMOOTH MUSCLE MYOSIN WITH REGULATORY LIGHT CHAIN IN THE DEPHOSPHORYLATED STATE. ONLY C ALPHAS PROVIDED FOR REGULATORY LIGHT CHAIN. ONLY BACKBONE ATOMS PROVIDED FOR S2 FRAGMENT.
Keywords keywords;muscle protein, smooth muscle, myosin subfragment 2, heavy meromyosin, essential light chain, regulatory light chain, motor protein, coiled-coil, CONTRACTILE PROTEIN ;; CONTRACTILE PROTEIN
Experimental Method methodELECTRON CRYSTALLOGRAPHY

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

Radius of gyration Rg (Guinier) rg_guinier54.89
Radius of gyration Rg (electron density) rg_electron54.63
Forward intensity I(0) i01008540000.00
Molecular weight molecular_weight262300.0 kDa
Excluded volume excluded_volume325900 ų
Envelope volume envelope_volume515700 ų
Hydration-shell volume shell_volume79918 ų
Envelope diameter envelope_diameter174.6
Shell Rg shell_rg55.96
Envelope Rg envelope_rg52.71
Shape Rg shape_rg52.83
Total Rg total_rg59.80
Total atoms total_atoms16304
Residues n_residues2106
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 dmax172.8
Rg (real space) rg_real54.76
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real1.0090e+09
I(0) uncertainty (real space) i0_real_error2.0510e+07
Rg (reciprocal space) rg_reciprocal54.97
I(0) (reciprocal space) i0_reciprocal1009000000.0000
Solution quality estimate total_estimate0.8845
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary77.5
Skewness Skewness skewness0.087
Kurtosis Kurtosis kurtosis-0.737
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha65440000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.604

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1i84s_
Class classi — Low resolution protein structures
Fold Fold foldi.15 — Muscle protein complexes
Superfamily Superfamily superfamilyi.15.1 — Muscle protein complexes
Family Family familyi.15.1.1 — Muscle protein complexes
Domain ID domain_idd1i84t_
Class classi — Low resolution protein structures
Fold Fold foldi.15 — Muscle protein complexes
Superfamily Superfamily superfamilyi.15.1 — Muscle protein complexes
Family Family familyi.15.1.1 — Muscle protein complexes
Domain ID domain_idd1i84u_
Class classi — Low resolution protein structures
Fold Fold foldi.15 — Muscle protein complexes
Superfamily Superfamily superfamilyi.15.1 — Muscle protein complexes
Family Family familyi.15.1.1 — Muscle protein complexes
Domain ID domain_idd1i84v_
Class classi — Low resolution protein structures
Fold Fold foldi.15 — Muscle protein complexes
Superfamily Superfamily superfamilyi.15.1 — Muscle protein complexes
Family Family familyi.15.1.1 — Muscle protein complexes
Domain ID domain_idd1i84w_
Class classi — Low resolution protein structures
Fold Fold foldi.15 — Muscle protein complexes
Superfamily Superfamily superfamilyi.15.1 — Muscle protein complexes
Family Family familyi.15.1.1 — Muscle protein complexes
Domain ID domain_idd1i84z_
Class classi — Low resolution protein structures
Fold Fold foldi.15 — Muscle protein complexes
Superfamily Superfamily superfamilyi.15.1 — Muscle protein complexes
Family Family familyi.15.1.1 — Muscle protein complexes

8. Citations (5)

9. Files and Curves (10)