6yel

Stromal interaction molecule 1 coiled-coil 1 fragment

Method: SOLUTION NMR Dmax: 71.4 Å Quality: REASONABLE

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

Stromal interaction molecule 1

Homo sapiens

UniProt Q13586

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 234–343 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.25;310.15 K;Ionic strength (raw mmCIF value) 0.02;Pressure 1 NMR sample composition:0.3 mM [U-98% 13C; U-98% 15N] STIM1 CC1, 20 mM TRIS, 7 mM [U-13C] SDS, 90 % v/v H2O, 10 % v/v [U-99% 2H] H2O, 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.

5 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STIM1_HUMAN
Isoform Q13586-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–115; UniProt 234–343

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 6yel

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6yel
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6yel
Deposition date deposition_date2020-03-25
Structure title titleStromal interaction molecule 1 coiled-coil 1 fragment
Keywords keywordsCalcium signaling, store-operated Ca2+ entry, CRAC, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.00
Radius of gyration Rg (electron density) rg_electron18.31
Forward intensity I(0) i01234550000.00
Molecular weight molecular_weight277770.0 kDa
Excluded volume excluded_volume340110 ų
Envelope volume envelope_volume36299 ų
Hydration-shell volume shell_volume15989 ų
Envelope diameter envelope_diameter76.2
Shell Rg shell_rg25.97
Envelope Rg envelope_rg21.44
Shape Rg shape_rg18.31
Total Rg total_rg18.39
Total atoms total_atoms38740
Residues n_residues2300
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 dmax71.4
Rg (real space) rg_real18.36
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real1.2350e+09
I(0) uncertainty (real space) i0_real_error1.8790e+07
Rg (reciprocal space) rg_reciprocal18.31
I(0) (reciprocal space) i0_reciprocal1235000000.0000
Solution quality estimate total_estimate0.7039
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.4
Skewness Skewness skewness0.671
Kurtosis Kurtosis kurtosis-0.102
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha448000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.332; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.154; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)