1yv0

Crystal structure of skeletal muscle troponin in the Ca2+-free state

Method: X-RAY DIFFRACTION Dmax: 96.3 Å Quality: GOOD

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

Troponin T, fast skeletal muscle isoforms

Gallus gallus

UniProt P12620

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain T; UniProt 156–262 Not recorded Troponin I, fast skeletal muscle × 1 (P68246) Troponin C, skeletal muscle × 1 (P02588) MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 7.00 Å R-free 0.359
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain T; UniProt 156–262 Not recorded Troponin I, fast skeletal muscle × 2 (P68246) Troponin C, skeletal muscle × 2 (P02588) MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 7.00 Å R-free 0.359

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNNT3_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain T; PDBConstruct 1–107; UniProt 156–262

Troponin I, fast skeletal muscle

Gallus gallus

UniProt P68246

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 1–137 Not recorded Troponin T, fast skeletal muscle isoforms × 1 (P12620) Troponin C, skeletal muscle × 1 (P02588) MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 7.00 Å R-free 0.359
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain I; UniProt 1–137 Not recorded Troponin T, fast skeletal muscle isoforms × 2 (P12620) Troponin C, skeletal muscle × 2 (P02588) MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 7.00 Å R-free 0.359

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNNI2_CHICK
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–137; UniProt 1–137

Troponin C, skeletal muscle

Gallus gallus

UniProt P02588

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–162 Not recorded Troponin T, fast skeletal muscle isoforms × 1 (P12620) Troponin I, fast skeletal muscle × 1 (P68246) MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 7.00 Å R-free 0.359
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–162 Not recorded Troponin T, fast skeletal muscle isoforms × 2 (P12620) Troponin I, fast skeletal muscle × 2 (P68246) MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;1.6 M tri-Sodium Citrate dihydrate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 7.00 Å R-free 0.359

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.

22 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNNC2_CHICK
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–162; UniProt 1–162

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 1yv0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1yv0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1yv0
Deposition date deposition_date2005-02-14
Structure title titleCrystal structure of skeletal muscle troponin in the Ca2+-free state
Keywords keywordstroponin, off state, thin filament, actin binding, muscle, 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_guinier29.15
Radius of gyration Rg (electron density) rg_electron28.27
Forward intensity I(0) i029617300.00
Molecular weight molecular_weight40554.0 kDa
Excluded volume excluded_volume50355 ų
Envelope volume envelope_volume74576 ų
Hydration-shell volume shell_volume23531 ų
Envelope diameter envelope_diameter100.8
Shell Rg shell_rg33.40
Envelope Rg envelope_rg27.80
Shape Rg shape_rg28.25
Total Rg total_rg28.90
Total atoms total_atoms2844
Residues n_residues349
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 dmax96.3
Rg (real space) rg_real29.13
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real2.9620e+07
I(0) uncertainty (real space) i0_real_error5.0260e+05
Rg (reciprocal space) rg_reciprocal29.14
I(0) (reciprocal space) i0_reciprocal29620000.0000
Solution quality estimate total_estimate0.8955
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.0
Skewness Skewness skewness0.179
Kurtosis Kurtosis kurtosis-0.567
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3952000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1yv0c1
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.5 — Calmodulin-like
Domain ID domain_idd1yv0i1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.25 — Troponin coil-coiled subunits
Family Family familyh.1.25.2 — Troponin I
Domain ID domain_idd1yv0t1
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.25 — Troponin coil-coiled subunits
Family Family familyh.1.25.1 — Troponin T

8. Citations (1)

9. Files and Curves (10)