2jv9

The Solution Structure of Calponin Homology Domain from Smoothelin-like 1

Method: SOLUTION NMR Dmax: 48.6 Å Quality: REASONABLE

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

Smoothelin-like 1

Mus musculus

UniProt Q99LM3

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 346–459 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;293 K;Ionic strength (raw mmCIF value) 0;Pressure ambient NMR measurement conditions:pH 7;293 K;Ionic strength (raw mmCIF value) 300;Pressure ambient NMR sample composition:0.5-1.0 mM [U-99% 13C; U-99% 15N] smoothelin-like 1, 1 mM sodium phosphate, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5-1.0 mM [U-99% 15N] smoothelin-like 1, 1 mM sodium phosphate, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5-1.0 mM smoothelin-like 1, 1 mM sodium phosphate, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 100% D2O | 100% D2O NMR sample composition:0.5-1.0 mM [U-99% 15N] smoothelin-like 1, 10 mg/mL Pf1 phage, 0.05 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 300 mM potassium chloride, 20 mM Bis-Tris, 90% H2O/10% D2O | 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 Q99LM3_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–119; UniProt 346–459

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 2jv9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2jv9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2jv9
Deposition date deposition_date2007-09-12
Structure title titleThe Solution Structure of Calponin Homology Domain from Smoothelin-like 1
Keywords keywordsCH-domain, Smoothelin, Smoothelin-like 1, Calponin, Calponin homology domain, STRUCTURAL PROTEIN, PROTEIN BINDING; STRUCTURAL PROTEIN, PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.13
Radius of gyration Rg (electron density) rg_electron13.88
Forward intensity I(0) i02249910000.00
Molecular weight molecular_weight410310.0 kDa
Excluded volume excluded_volume515570 ų
Envelope volume envelope_volume32726 ų
Hydration-shell volume shell_volume16457 ų
Envelope diameter envelope_diameter57.7
Shell Rg shell_rg23.01
Envelope Rg envelope_rg17.30
Shape Rg shape_rg13.83
Total Rg total_rg14.17
Total atoms total_atoms57450
Residues n_residues3570
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 dmax48.6
Rg (real space) rg_real14.02
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real2.2500e+09
I(0) uncertainty (real space) i0_real_error2.3620e+07
Rg (reciprocal space) rg_reciprocal14.03
I(0) (reciprocal space) i0_reciprocal2250000000.0000
Solution quality estimate total_estimate0.7490
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.8
Skewness Skewness skewness0.105
Kurtosis Kurtosis kurtosis-0.115
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha494100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.579; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2jv9a1
Class classa — All alpha proteins
Fold Fold folda.40 — CH domain-like
Superfamily Superfamily superfamilya.40.1 — Calponin-homology domain, CH-domain
Family Family familya.40.1.0 — automated matches
Domain ID domain_idd2jv9a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2jv9A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily10 — Calponin-like domain

8. Citations (1)

9. Files and Curves (10)