SAXSdb — 2bv1

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

REGULATOR OF G-PROTEIN SIGNALLING 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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 50–192	Fragment：RESIDUES 50-192	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；4.1M SODIUM FORMATE, 3% GLYCEROL. 1:1 MIXTURE WITH RGS1 PROTEIN AT 23MG/ML., pH 8.00	Resolution 2.00 Å R-free 0.241
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 50–192	Fragment：RESIDUES 50-192	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；4.1M SODIUM FORMATE, 3% GLYCEROL. 1:1 MIXTURE WITH RGS1 PROTEIN AT 23MG/ML., pH 8.00	Resolution 2.00 Å R-free 0.241

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 2BV1	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2GTP Crystal structure of the heterodimeric complex of human RGS1 and activated Gi alpha 1 Deposited 2006-04-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 50–192（143 aa）	Not recorded	ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.2M NaNO3, 0.1M bis-Tris propane, pH 6.5, 20 % PEG3350, 10 % Ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.55 Å R-free 0.276
2GTP Crystal structure of the heterodimeric complex of human RGS1 and activated Gi alpha 1 Deposited 2006-04-28	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 50–192（143 aa）	Not recorded	ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.2M NaNO3, 0.1M bis-Tris propane, pH 6.5, 20 % PEG3350, 10 % Ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.55 Å R-free 0.276

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RGS1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–145； UniProt 50–192 Author chain B； PDBConstruct 3–145； UniProt 50–192

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	2bv1
Deposition date deposition_date	2005-06-20
Structure title title	Regulator of G-protein Signalling 1 (Human)
Keywords keywords	;RGS1, RGS, G-PROTEIN, REGULATOR, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, B-CELL ACTIVATION, PHOSPHORYLATION, SIGNAL TRANSDUCTION INHIBITOR, 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	22.74 Å
Radius of gyration Rg (electron density) rg_electron	21.97 Å
Forward intensity I(0) i0	15127300.00
Molecular weight molecular_weight	29728.0 kDa
Excluded volume excluded_volume	37327 Å³
Envelope volume envelope_volume	45165 Å³
Hydration-shell volume shell_volume	18267 Å³
Envelope diameter envelope_diameter	77.9 Å
Shell Rg shell_rg	27.64 Å
Envelope Rg envelope_rg	22.29 Å
Shape Rg shape_rg	21.92 Å
Total Rg total_rg	22.93 Å
Total atoms total_atoms	2096
Residues n_residues	264
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	78.4 Å
Rg (real space) rg_real	22.84 Å
Rg uncertainty (real space) rg_real_error	0.82 Å
I(0) (real space) i0_real	1.5130e+07
I(0) uncertainty (real space) i0_real_error	2.2860e+05
Rg (reciprocal space) rg_reciprocal	22.82 Å
I(0) (reciprocal space) i0_reciprocal	15130000.0000
Solution quality estimate total_estimate	0.8638
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.4 Å
Skewness Skewness skewness	0.426
Kurtosis Kurtosis kurtosis	-0.327
Angular range angular_range	— – 0.3500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4317000.0000
Real-space data points n_real_points	67
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.795; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.859; Smooth: 0.987

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2bv1a_
Class class	a — All alpha proteins
Fold Fold fold	a.91 — Regulator of G-protein signaling, RGS
Superfamily Superfamily superfamily	a.91.1 — Regulator of G-protein signaling, RGS
Family Family family	a.91.1.0 — automated matches

Domain ID domain_id	d2bv1b_
Class class	a — All alpha proteins
Fold Fold fold	a.91 — Regulator of G-protein signaling, RGS
Superfamily Superfamily superfamily	a.91.1 — Regulator of G-protein signaling, RGS
Family Family family	a.91.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id	2bv1A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	196 — Regulator of G-protein Signalling 4; domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2bv1A02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	167 — Regulator of G-protein Signalling 4; domain 2
Homologous superfamily homologous superfamily	10 — Regulator of G-protein Signalling 4, domain 2

Domain ID domain_id	2bv1B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	196 — Regulator of G-protein Signalling 4; domain 1
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	2bv1B02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	167 — Regulator of G-protein Signalling 4; domain 2
Homologous superfamily homologous superfamily	10 — Regulator of G-protein Signalling 4, domain 2

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8. Citations (1)

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Unit-cell length a length_a	40.738 Å
Unit-cell length b length_b	43.202 Å
Unit-cell length c length_c	58.651 Å
Unit-cell angle α angle_alpha	78.43 °
Unit-cell angle β angle_beta	85.30 °
Unit-cell angle γ angle_gamma	69.74 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	57.450 Å
R factor r_factor	0.1910
R_work r_work	0.1880
R_free r_free	0.2410

Description description	REGULATOR OF G-PROTEIN SIGNALLING 1
Molecular weight formula_weight	16575.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2263

Regulator of G-protein Signalling 1 (Human)

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

REGULATOR OF G-PROTEIN SIGNALLING 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

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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 BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	155

fit	/app/data/saxs_computation/bv/2bv1/2bv1.fit
pddf	/app/data/pr_computation/bv/2bv1/2bv1.pr.out
profile	/app/data/saxs_computation/bv/2bv1/2bv1.dat