1pon

SITE III-SITE IV TROPONIN C HETERODIMER, NMR

Method: SOLUTION NMR Dmax: 41.6 Å Quality: GOOD

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

TROPONIN C

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 93–126 Chain B; UniProt 129–162 Fragment:SITE III AND IV Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPCS_CHICK
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 2–35; UniProt 93–126 Author chain B; PDBConstruct 2–35; UniProt 129–162

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 1pon

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1pon
Deposition date deposition_date1996-04-02
Structure title titleSITE III-SITE IV TROPONIN C HETERODIMER, NMR
Keywords keywordsEF-HAND, MUSCLE PROTEIN, CALCIUM-BINDING PROTEIN; CALCIUM-BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.22
Radius of gyration Rg (electron density) rg_electron12.87
Forward intensity I(0) i01704510000.00
Molecular weight molecular_weight332080.0 kDa
Excluded volume excluded_volume407000 ų
Envelope volume envelope_volume27856 ų
Hydration-shell volume shell_volume15072 ų
Envelope diameter envelope_diameter51.6
Shell Rg shell_rg21.54
Envelope Rg envelope_rg15.72
Shape Rg shape_rg12.84
Total Rg total_rg13.05
Total atoms total_atoms45192
Residues n_residues2856
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 dmax41.6
Rg (real space) rg_real13.13
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real1.7050e+09
I(0) uncertainty (real space) i0_real_error1.5920e+07
Rg (reciprocal space) rg_reciprocal13.14
I(0) (reciprocal space) i0_reciprocal1705000000.0000
Solution quality estimate total_estimate0.8186
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.3
Skewness Skewness skewness0.068
Kurtosis Kurtosis kurtosis-0.355
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha91680.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1pon.1
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

8. Citations (2)

9. Files and Curves (10)