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2maj

Solution Structure of the STIM1 CC1-CC2 homodimer.

Method: SOLUTION NMR Dmax: 52.5 Å Quality: REASONABLE
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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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 312–387 Chain C； UniProt 312–387 Fragment：UNP residues 312-387 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5.5；308 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient NMR sample composition：0.5 mM [U-99% 15N] protein, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：0.5 mM [U-99% 13C; U-99% 15N] protein, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition：0.5 mM [U-99% 13C; U-99% 15N] protein, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 100% D2O | 100% D2O NMR sample composition：0.5 mM [U-99% 13C; U-99% 15N] protein, 0.5 mM protein, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 100% D2O | 100% 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.

Other PDB Difference from Current Entry 2MAJ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2K60 NMR structure of calcium-loaded STIM1 EF-SAM Deposited 2008-07-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 58–201（144 aa） Fragment：UNP residues 58-201
Not recorded CA CALCIUM ION × 1 SOLUTION NMR
NMR measurement conditions pH 8；293 K；Ionic strength (raw mmCIF value) 105；Pressure 1
NMR measurement conditions 293 K；Ionic strength (raw mmCIF value) 105；Pressure 1
NMR sample composition 0.5-1.0 mM [U-100% 13C; U-100% 15N] stromal interaction molecule 1, 20 mM TRIS, 100 mM sodium chloride, 5 mM CALCIUM ION, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.5-1.0 mM [U-100% 13C; U-100% 15N] stromal interaction molecule 1, 20 mM [U-99% 2H] TRIS, 100 mM sodium chloride, 5 mM CALCIUM ION, 100% D2O | 100% D2O
Resolution not provided
2MAK Solution structure of the STIM1 CC1-CC2 homodimer in complex with two Orai1 C-terminal domains. Deposited 2013-07-12 Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 312–387（76 aa） Fragment：UNP residues 312-387
Chain C 312–387（76 aa） Fragment：UNP residues 312-387
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient
NMR sample composition 0.25 mM [U-100% 15N] protein_1, 3.0 mM protein_2, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.25 mM [U-99% 13C; U-99% 15N] protein_1, 3.0 mM protein_2, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.25 mM [U-99% 13C; U-99% 15N] protein_1, 3.0 mM protein_2, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 100% D2O | 100% D2O
NMR sample composition 2.5 mM protein_1, 0.25 mM [U-99% 15N] protein_2, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 2.5 mM protein_1, 0.25 mM [U-99% 13C; U-99% 15N] protein_2, 20 mM bis-TRIS, 0.175 v/v [U-99% 2H] TFE, 100% D2O | 100% D2O
Resolution not provided
3TEQ Crystal structure of SOAR domain Deposited 2011-08-15 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 344–444（101 aa） Fragment：SOAR domain (UNP RESIDUES 344-444)
Chain C 344–444（101 aa） Fragment：SOAR domain (UNP RESIDUES 344-444)
Mutation：L374M, V419A, C437T Mutation：L374M, V419A, C437T PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；0.1M Bis-Tris pH 6.5, 10% PEG3350, 0.2M Ammonium dibasic phosphate, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.90 Å R-free 0.249
3TEQ Crystal structure of SOAR domain Deposited 2011-08-15 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 344–444（101 aa） Fragment：SOAR domain (UNP RESIDUES 344-444)
Mutation：L374M, V419A, C437T No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；0.1M Bis-Tris pH 6.5, 10% PEG3350, 0.2M Ammonium dibasic phosphate, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.90 Å R-free 0.249
3TEQ Crystal structure of SOAR domain Deposited 2011-08-15 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain D 344–444（101 aa） Fragment：SOAR domain (UNP RESIDUES 344-444)
Mutation：L374M, V419A, C437T No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；0.1M Bis-Tris pH 6.5, 10% PEG3350, 0.2M Ammonium dibasic phosphate, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.90 Å R-free 0.249
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain D 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Mutation：M244L, L321M Mutation：M244L, L321M CD CADMIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；24% PEGMME 2000, 0.1M sodium acetate, 0.02M magnesium chloride hexahydrate, 0.02M nickel chloride hexahydrate, 0.02M cadmium chloride hexahydrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.289
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain C 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Mutation：M244L, L321M Mutation：M244L, L321M CD CADMIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；24% PEGMME 2000, 0.1M sodium acetate, 0.02M magnesium chloride hexahydrate, 0.02M nickel chloride hexahydrate, 0.02M cadmium chloride hexahydrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.289
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain B 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Mutation：M244L, L321M Mutation：M244L, L321M CD CADMIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；24% PEGMME 2000, 0.1M sodium acetate, 0.02M magnesium chloride hexahydrate, 0.02M nickel chloride hexahydrate, 0.02M cadmium chloride hexahydrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.289
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain D 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Mutation：M244L, L321M Mutation：M244L, L321M CD CADMIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；24% PEGMME 2000, 0.1M sodium acetate, 0.02M magnesium chloride hexahydrate, 0.02M nickel chloride hexahydrate, 0.02M cadmium chloride hexahydrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.289
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain B 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain C 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Chain D 237–340（104 aa） Fragment：CC1-IH, UNP RESIDUES 237-340
Mutation：M244L, L321M Mutation：M244L, L321M Mutation：M244L, L321M Mutation：M244L, L321M CD CADMIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；24% PEGMME 2000, 0.1M sodium acetate, 0.02M magnesium chloride hexahydrate, 0.02M nickel chloride hexahydrate, 0.02M cadmium chloride hexahydrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.289
6YEL Stromal interaction molecule 1 coiled-coil 1 fragment Deposited 2020-03-25 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 234–343（110 aa）
Not recorded No recorded non-water small molecule 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

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 —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 7–82； UniProt 312–387 Author chain C； PDBConstruct 7–82； UniProt 312–387

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 2maj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2maj
Deposition date deposition_date2013-07-12
Structure title titleSolution Structure of the STIM1 CC1-CC2 homodimer.
Keywords keywordsSTIM1, coiled-coil, TRANSPORT PROTEIN, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.08 Å
Radius of gyration Rg (electron density) rg_electron19.40 Å
Forward intensity I(0) i02113090000.00
Molecular weight molecular_weight387440.0 kDa
Excluded volume excluded_volume484290 ų
Envelope volume envelope_volume44970 ų
Hydration-shell volume shell_volume18107 ų
Envelope diameter envelope_diameter91.8 Å
Shell Rg shell_rg28.15 Å
Envelope Rg envelope_rg23.97 Å
Shape Rg shape_rg19.33 Å
Total Rg total_rg19.77 Å
Total atoms total_atoms54880
Residues n_residues3280
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax52.5 Å
Rg (real space) rg_real17.85 Å
Rg uncertainty (real space) rg_real_error0.11 Å
I(0) (real space) i0_real2.0170e+09
I(0) uncertainty (real space) i0_real_error1.9810e+07
Rg (reciprocal space) rg_reciprocal19.38 Å
I(0) (reciprocal space) i0_reciprocal2113000000.0000
Solution quality estimate total_estimate0.6697
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.5 Å
Skewness Skewness skewness0.468
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.4150 Å−1
Current regularization parameter α current_alpha2.9470
Highest regularization parameter α highest_alpha1392000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.922; Stabil: 0.993; Sysdev: 0.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)