1cmz

SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR OF G PROTEIN SIGNALING

Method: SOLUTION NMR D_max: 53.3 Å Quality: GOOD

▼

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

PROTEIN (GAIP (G-ALPHA INTERACTING) PROTEIN)

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 68–217	Fragment：RGS BOX	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 7.2；300 K NMR measurement conditions：pH 8.3；300 K NMR sample composition：90% WATER/10% 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	RGS19_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–152； UniProt 68–217

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1cmz
Deposition date deposition_date	1999-05-12
Structure title title	SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR OF G PROTEIN SIGNALING
Keywords keywords	GAIP, RGS, REGULATOR OF G PROTEIN, SIGNALING PROTEIN REGULATION; SIGNALING PROTEIN REGULATION
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	16.35 Å
Radius of gyration Rg (electron density) rg_electron	16.23 Å
Forward intensity I(0) i0	1258730000.00
Molecular weight molecular_weight	298460.0 kDa
Excluded volume excluded_volume	371710 Å³
Envelope volume envelope_volume	32123 Å³
Hydration-shell volume shell_volume	15903 Å³
Envelope diameter envelope_diameter	58.5 Å
Shell Rg shell_rg	23.05 Å
Envelope Rg envelope_rg	17.55 Å
Shape Rg shape_rg	16.22 Å
Total Rg total_rg	16.36 Å
Total atoms total_atoms	41380
Residues n_residues	2560
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

▼

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

Maximum dimension Dmax dmax	53.3 Å
Rg (real space) rg_real	16.38 Å
Rg uncertainty (real space) rg_real_error	0.32 Å
I(0) (real space) i0_real	1.2590e+09
I(0) uncertainty (real space) i0_real_error	1.4530e+07
Rg (reciprocal space) rg_reciprocal	16.38 Å
I(0) (reciprocal space) i0_reciprocal	1259000000.0000
Solution quality estimate total_estimate	0.8617
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.1 Å
Skewness Skewness skewness	0.358
Kurtosis Kurtosis kurtosis	-0.380
Angular range angular_range	— – 0.4850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	528900.0000
Real-space data points n_real_points	79
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.741; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.982

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1cmza_
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.91.1.1 — Regulator of G-protein signaling, RGS

CATH v4.4 (2 domains)

Domain ID domain_id	1cmzA01
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	1cmzA02
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

▶

8. Citations (2)

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

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

Description description	PROTEIN (GAIP (G-ALPHA INTERACTING) PROTEIN)
Molecular weight formula_weight	17286.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	41380

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)

SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR OF G PROTEIN SIGNALING

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

PROTEIN (GAIP (G-ALPHA INTERACTING) PROTEIN)

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/cm/1cmz/1cmz.fit
pddf	/app/data/pr_computation/cm/1cmz/1cmz.pr.out
profile	/app/data/saxs_computation/cm/1cmz/1cmz.dat