1npq

structure of a rhodamine-labeled N-domain Troponin C mutant (Ca2+ saturated) in complex with skeletal Troponin I 115-131

Method: SOLUTION NMR Dmax: 50.4 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–90 Fragment:TnC, residues 1-90 Mutation:E56C, E63C Troponin I × 1 (P02643) CA CALCIUM ION × 2 SOLUTION NMR NMR measurement conditions:pH 6.5;303 K;Ionic strength (raw mmCIF value) 320 mM KCl;Pressure ambiant NMR sample composition:320 mM KCl, 10 mM imidazole, 1.3% NaN3, pH 6.5, ~1mM sNTnC.2Ca2+.TnI115-131.BR56-63 | 90% H2O/10% D2O 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 TNNC2_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–90; UniProt 1–90

Troponin I

OrganismNot specified

UniProt P02643

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 115–131 Fragment:switch peptide, residues 115-131 Troponin C × 1 (P02588) CA CALCIUM ION × 2 SOLUTION NMR NMR measurement conditions:pH 6.5;303 K;Ionic strength (raw mmCIF value) 320 mM KCl;Pressure ambiant NMR sample composition:320 mM KCl, 10 mM imidazole, 1.3% NaN3, pH 6.5, ~1mM sNTnC.2Ca2+.TnI115-131.BR56-63 | 90% H2O/10% D2O 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNNI2_RABIT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–17; UniProt 115–131

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 1npq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1npq
Deposition date deposition_date2003-01-18
Structure title titlestructure of a rhodamine-labeled N-domain Troponin C mutant (Ca2+ saturated) in complex with skeletal Troponin I 115-131
Keywords keywordsTroponin C- Troponin I complex, bifunctional rhodamine labeled Toponin C, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.67
Radius of gyration Rg (electron density) rg_electron13.17
Forward intensity I(0) i0972665000.00
Molecular weight molecular_weight249470.0 kDa
Excluded volume excluded_volume305880 ų
Envelope volume envelope_volume31084 ų
Hydration-shell volume shell_volume15843 ų
Envelope diameter envelope_diameter58.3
Shell Rg shell_rg22.71
Envelope Rg envelope_rg17.16
Shape Rg shape_rg13.16
Total Rg total_rg13.41
Total atoms total_atoms33936
Residues n_residues2247
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 dmax50.4
Rg (real space) rg_real13.59
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real9.7270e+08
I(0) uncertainty (real space) i0_real_error1.1430e+07
Rg (reciprocal space) rg_reciprocal13.60
I(0) (reciprocal space) i0_reciprocal972700000.0000
Solution quality estimate total_estimate0.8049
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.5
Skewness Skewness skewness0.176
Kurtosis Kurtosis kurtosis-0.053
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha364300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.494; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1npqa_
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

CATH v4.4 (1 domains)

Domain ID domain_id1npqA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (1)

9. Files and Curves (10)