3bat

Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (P21) form

Method: X-RAY DIFFRACTION Dmax: 128.3 Å Quality: REASONABLE

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

Myosin heavy chain, striated muscle/General control protein GCN4

Saccharomyces cerevisiae

UniProt P03069

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 250–281 Chain B; UniProt 250–281 Fragment:Bay Scallop Myosin (Residues 835-885)/Yeast GCN4 Transcription Factor (Residues 250-281) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;277 K;2 microliters of protein solution (4 mg/ml protein in 30 mM MOPS buffer pH 7.2, 40 mM NaCl, 2 mM NaN3) mixed with 2 microliters of (25% PEG 3350, 50 mM NH4I) and equilibrated against 1 ml of (17.5% PEG 3350, 35 mM NH4I, 28 mM NaCl, 2 mM NaN3, 20 mM MOPS pH 6.2). Harvested crystals were cryoprotected in 25.5% PEG 3350 and 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.30 Å R-free 0.299
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 250–281 Chain D; UniProt 250–281 Fragment:Bay Scallop Myosin (Residues 835-885)/Yeast GCN4 Transcription Factor (Residues 250-281) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;277 K;2 microliters of protein solution (4 mg/ml protein in 30 mM MOPS buffer pH 7.2, 40 mM NaCl, 2 mM NaN3) mixed with 2 microliters of (25% PEG 3350, 50 mM NH4I) and equilibrated against 1 ml of (17.5% PEG 3350, 35 mM NH4I, 28 mM NaCl, 2 mM NaN3, 20 mM MOPS pH 6.2). Harvested crystals were cryoprotected in 25.5% PEG 3350 and 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.30 Å R-free 0.299

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.

162 other PDB entries and 199 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCN4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 58–89; UniProt 250–281 Author chain B; PDBConstruct 58–89; UniProt 250–281 Author chain C; PDBConstruct 58–89; UniProt 250–281 Author chain D; PDBConstruct 58–89; UniProt 250–281

Myosin heavy chain, striated muscle/General control protein GCN4

Saccharomyces cerevisiae

UniProt P24733

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 835–885 Chain B; UniProt 835–885 Fragment:Bay Scallop Myosin (Residues 835-885)/Yeast GCN4 Transcription Factor (Residues 250-281) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;277 K;2 microliters of protein solution (4 mg/ml protein in 30 mM MOPS buffer pH 7.2, 40 mM NaCl, 2 mM NaN3) mixed with 2 microliters of (25% PEG 3350, 50 mM NH4I) and equilibrated against 1 ml of (17.5% PEG 3350, 35 mM NH4I, 28 mM NaCl, 2 mM NaN3, 20 mM MOPS pH 6.2). Harvested crystals were cryoprotected in 25.5% PEG 3350 and 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.30 Å R-free 0.299
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 835–885 Chain D; UniProt 835–885 Fragment:Bay Scallop Myosin (Residues 835-885)/Yeast GCN4 Transcription Factor (Residues 250-281) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;277 K;2 microliters of protein solution (4 mg/ml protein in 30 mM MOPS buffer pH 7.2, 40 mM NaCl, 2 mM NaN3) mixed with 2 microliters of (25% PEG 3350, 50 mM NH4I) and equilibrated against 1 ml of (17.5% PEG 3350, 35 mM NH4I, 28 mM NaCl, 2 mM NaN3, 20 mM MOPS pH 6.2). Harvested crystals were cryoprotected in 25.5% PEG 3350 and 15% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.30 Å R-free 0.299

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.

19 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYS_AEQIR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–55; UniProt 835–885 Author chain B; PDBConstruct 5–55; UniProt 835–885 Author chain C; PDBConstruct 5–55; UniProt 835–885 Author chain D; PDBConstruct 5–55; UniProt 835–885

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 3bat

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3bat
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3bat
Deposition date deposition_date2007-11-08
Structure title titleCrystal structure of the N-terminal region of the scallop myosin rod, monoclinic (P21) form
Keywords keywords;Alpha-helical coiled coil, disorder, salt links, contractile protein, Actin-binding, ATP-binding, Calmodulin-binding, Cytoplasm, Motor protein, Muscle protein, Myosin, Nucleotide-binding, Thick filament ;; CONTRACTILE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.53
Radius of gyration Rg (electron density) rg_electron36.21
Forward intensity I(0) i025017400.00
Molecular weight molecular_weight38597.0 kDa
Excluded volume excluded_volume48231 ų
Envelope volume envelope_volume71907 ų
Hydration-shell volume shell_volume19515 ų
Envelope diameter envelope_diameter129.4
Shell Rg shell_rg35.08
Envelope Rg envelope_rg36.76
Shape Rg shape_rg36.14
Total Rg total_rg36.33
Total atoms total_atoms2694
Residues n_residues323
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 dmax128.3
Rg (real space) rg_real36.23
Rg uncertainty (real space) rg_real_error1.75
I(0) (real space) i0_real2.5020e+07
I(0) uncertainty (real space) i0_real_error4.5810e+05
Rg (reciprocal space) rg_reciprocal35.80
I(0) (reciprocal space) i0_reciprocal25010000.0000
Solution quality estimate total_estimate0.5342
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.627
Kurtosis Kurtosis kurtosis-0.396
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1490000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.489; Stabil: 1.000; Sysdev: 0.186; Positv: 1.000; Valcen: 0.203; Smooth: 0.710

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3batA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340
Domain ID domain_id3batB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340
Domain ID domain_id3batC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340
Domain ID domain_id3batD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340

8. Citations (3)

9. Files and Curves (10)