1c1g

CRYSTAL STRUCTURE OF TROPOMYOSIN AT 7 ANGSTROMS RESOLUTION IN THE SPERMINE-INDUCED CRYSTAL FORM

Method: X-RAY DIFFRACTION Dmax: 267.8 Å Quality: REASONABLE

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

TROPOMYOSIN

OrganismNot specified

UniProt P42639

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–284 Chain B; UniProt 1–284 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:LIQUID DIFFUSION;pH 7.4;291 K;SPERMINE, pH 7.4, LIQUID DIFFUSION, temperature 18K Resolution 7.00 Å
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–284 Chain D; UniProt 1–284 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:LIQUID DIFFUSION;pH 7.4;291 K;SPERMINE, pH 7.4, LIQUID DIFFUSION, temperature 18K Resolution 7.00 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.

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

View Construct and Data Evidence
UniProt name TPM1_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–284; UniProt 1–284 Author chain B; PDBConstruct 1–284; UniProt 1–284 Author chain C; PDBConstruct 1–284; UniProt 1–284 Author chain D; PDBConstruct 1–284; UniProt 1–284

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 1c1g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c1g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c1g
Deposition date deposition_date1999-07-22
Structure title titleCRYSTAL STRUCTURE OF TROPOMYOSIN AT 7 ANGSTROMS RESOLUTION IN THE SPERMINE-INDUCED CRYSTAL FORM
Keywords keywordsTROPOMYOSIN COILED-COIL ALPHA-HELICAL, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron134.60
Forward intensity I(0) i0264136000.00
Molecular weight molecular_weight130810.0 kDa
Excluded volume excluded_volume161950 ų
Envelope volume envelope_volume339530 ų
Hydration-shell volume shell_volume32495 ų
Envelope diameter envelope_diameter528.7
Shell Rg shell_rg49.32
Envelope Rg envelope_rg141.60
Shape Rg shape_rg134.20
Total Rg total_rg134.30
Total atoms total_atoms9160
Residues n_residues1136
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 dmax267.8
Rg (real space) rg_real92.38
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real2.1970e+08
I(0) uncertainty (real space) i0_real_error4.8380e+06
Rg (reciprocal space) rg_reciprocal93.51
I(0) (reciprocal space) i0_reciprocal239400000.0000
Solution quality estimate total_estimate0.6720
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.7
Skewness Skewness skewness0.296
Kurtosis Kurtosis kurtosis-1.061
Angular range angular_range— – 0.0550 −1
Current regularization parameter α current_alpha3.3430
Highest regularization parameter α highest_alpha35790000.0000
Real-space data points n_real_points12
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.206; Oscil: 0.536; Stabil: 0.787; Sysdev: 1.000; Positv: 1.000; Valcen: 0.767; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1c1ga_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.5 — Tropomyosin
Family Family familyh.1.5.1 — Tropomyosin
Domain ID domain_idd1c1gb_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.5 — Tropomyosin
Family Family familyh.1.5.1 — Tropomyosin
Domain ID domain_idd1c1gc_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.5 — Tropomyosin
Family Family familyh.1.5.1 — Tropomyosin
Domain ID domain_idd1c1gd_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.5 — Tropomyosin
Family Family familyh.1.5.1 — Tropomyosin

8. Citations (1)

9. Files and Curves (10)