2k3s

HADDOCK-derived structure of the CH-domain of the smoothelin-like 1 complexed with the C-domain of apocalmodulin

Method: SOLUTION NMR Dmax: 61.5 Å Quality: GOOD

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

Smoothelin-like protein 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 346–459 Not recorded Calmodulin × 1 (P62155) SOLUTION NMR NMR measurement conditions:pH 7;293 K;Ionic strength (raw mmCIF value) 0;Pressure ambient NMR sample composition:0.5 mM [U-100% 15N] entity_1, 0.6 mM calmodulin (full length), 20 mM Bis-Tris, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 1 mM EDTA, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.6 mM entity_1, 0.5 mM [U-100% 15N] calmodulin (full length), 20 mM Bis-Tris, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 1 mM EDTA, 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 SMTL1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–119; UniProt 346–459

Calmodulin

Xenopus laevis

UniProt P62155

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 83–149 Not recorded Smoothelin-like protein 1 × 1 (Q99LM3) SOLUTION NMR NMR measurement conditions:pH 7;293 K;Ionic strength (raw mmCIF value) 0;Pressure ambient NMR sample composition:0.5 mM [U-100% 15N] entity_1, 0.6 mM calmodulin (full length), 20 mM Bis-Tris, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 1 mM EDTA, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.6 mM entity_1, 0.5 mM [U-100% 15N] calmodulin (full length), 20 mM Bis-Tris, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 1 mM EDTA, 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.

22 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–67; UniProt 83–149

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 2k3s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2k3s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2k3s
Deposition date deposition_date2008-05-15
Structure title titleHADDOCK-derived structure of the CH-domain of the smoothelin-like 1 complexed with the C-domain of apocalmodulin
Keywords keywords;apocalmodulin complex, calponin homology domain, smoothelin-like 1, HADDOCK model, CH-domain, Coiled coil, Acetylation, Calcium, Methylation, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.96
Radius of gyration Rg (electron density) rg_electron18.70
Forward intensity I(0) i01485120000.00
Molecular weight molecular_weight320910.0 kDa
Excluded volume excluded_volume398680 ų
Envelope volume envelope_volume49100 ų
Hydration-shell volume shell_volume20555 ų
Envelope diameter envelope_diameter69.7
Shell Rg shell_rg26.57
Envelope Rg envelope_rg20.54
Shape Rg shape_rg18.66
Total Rg total_rg18.94
Total atoms total_atoms27600
Residues n_residues2790
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 dmax61.5
Rg (real space) rg_real19.02
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real1.4850e+09
I(0) uncertainty (real space) i0_real_error1.7550e+07
Rg (reciprocal space) rg_reciprocal19.01
I(0) (reciprocal space) i0_reciprocal1485000000.0000
Solution quality estimate total_estimate0.7915
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.422
Kurtosis Kurtosis kurtosis-0.343
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1434000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.779; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2k3sa1
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_idd2k3sa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2k3sb1
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_id2k3sA01
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)