SAXSdb — 3teq

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

Stromal interaction molecule 1

Homo sapiens

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 344–444 Chain C； UniProt 344–444	Fragment：SOAR domain (UNP RESIDUES 344-444) 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
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 344–444	Fragment：SOAR domain (UNP RESIDUES 344-444) Mutation：L374M, V419A, C437T	No other associated polymer	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
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 344–444	Fragment：SOAR domain (UNP RESIDUES 344-444) Mutation：L374M, V419A, C437T	No other associated polymer	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

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 3TEQ	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 method Different experimental conditions Different structure-quality metrics	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
2MAJ Solution Structure of the STIM1 CC1-CC2 homodimer. Deposited 2013-07-12	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	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 0.5 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
2MAK Solution structure of the STIM1 CC1-CC2 homodimer in complex with two Orai1 C-terminal domains. Deposited 2013-07-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	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
4O9B The Structure of CC1-IH in human STIM1. Deposited 2014-01-02	Different construct Different mutation/modification Different ligand/ion 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 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 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 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 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 method Different experimental conditions Different structure-quality metrics	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 9 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 1–101； UniProt 344–444 Author chain B； PDBConstruct 1–101； UniProt 344–444 Author chain C； PDBConstruct 1–101； UniProt 344–444 Author chain D； PDBConstruct 1–101； UniProt 344–444

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3teq
Deposition date deposition_date	2011-08-15
Structure title title	Crystal structure of SOAR domain
Keywords keywords	SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	32.12 Å
Radius of gyration Rg (electron density) rg_electron	32.99 Å
Forward intensity I(0) i0	36850500.00
Molecular weight molecular_weight	46886.0 kDa
Excluded volume excluded_volume	58652 Å³
Envelope volume envelope_volume	82359 Å³
Hydration-shell volume shell_volume	24626 Å³
Envelope diameter envelope_diameter	121.9 Å
Shell Rg shell_rg	33.06 Å
Envelope Rg envelope_rg	33.76 Å
Shape Rg shape_rg	33.04 Å
Total Rg total_rg	32.83 Å
Total atoms total_atoms	3303
Residues n_residues	402
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	115.7 Å
Rg (real space) rg_real	32.51 Å
Rg uncertainty (real space) rg_real_error	1.44 Å
I(0) (real space) i0_real	3.6850e+07
I(0) uncertainty (real space) i0_real_error	5.9910e+05
Rg (reciprocal space) rg_reciprocal	32.35 Å
I(0) (reciprocal space) i0_reciprocal	36850000.0000
Solution quality estimate total_estimate	0.8267
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	28.3 Å
Skewness Skewness skewness	0.517
Kurtosis Kurtosis kurtosis	-0.231
Angular range angular_range	— – 0.2450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2319000.0000
Real-space data points n_real_points	50
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.766; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.606; Smooth: 0.839

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Stromal interaction molecule 1
Molecular weight formula_weight	11713.4 kDa
Mutation mutation	L374M, V419A, C437T
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	3886

PEALQKWLQLTHEVEVQYYNIKKQNAEKQLMVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEATAALRERLHRWQQIEILTGFQIVNN

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	583

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7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	3teqA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	3550 —

Domain ID domain_id	3teqB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	3550 —

Domain ID domain_id	3teqC00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	3550 —

Domain ID domain_id	3teqD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	3550 —

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8. Citations (1)

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Unit-cell length a length_a	90.584 Å
Unit-cell length b length_b	90.584 Å
Unit-cell length c length_c	104.919 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	32

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	25.200 Å
R factor r_factor	0.2190
R_work r_work	0.2190
R_free r_free	0.2490

fit	/app/data/saxs_computation/te/3teq/3teq.fit
pddf	/app/data/pr_computation/te/3teq/3teq.pr.out
profile	/app/data/saxs_computation/te/3teq/3teq.dat

Crystal structure of SOAR domain

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

Stromal interaction molecule 1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement