SAXSdb — 1cxx

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

CYSTEINE AND GLYCINE-RICH PROTEIN CRP2

Coturnix japonica

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 82–194	Fragment：CARBOXYL-TERMINAL LIM-DOMAIN Mutation：R122A	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions：pH 7；299 K；Pressure AMBIENT NMR sample composition：1.1MM QCRP2(LIM2)R122A 15N; 20MM POTASSIUM PHOSPHATE; 50MM POTASSIUM CHLORIDE; 0.5MM DTT;	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 1CXX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A7I AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1998-03-15	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–80（80 aa） Fragment：N-TERMINAL LIM DOMAIN	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 7.2；299 K	Resolution not provided
1IBI QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, 15 MINIMIZED MODEL STRUCTURES Deposited 2001-03-28	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–193（113 aa） Fragment：C-TERMINAL LIM DOMAIN, RESIDUES 82-194	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 7.2；299 K；Ionic strength (raw mmCIF value) 20mM potassium phosphate; 50mM KCl；Pressure ambient NMR sample composition 1-2mM qCRP2(LIM2) U-15N,13C; 20 mM potassium phosphate, 50mM KCl, 0.5mM dithiothreitol, 90% H2O, 10% D2O \| 90% H2O/10% D2O NMR sample composition 1-2mM qCRP2(LIM2) U-15N; 20 mM potassium phosphate, 50mM KCl, 0.5mM dithiothreitol, 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
1QLI QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1997-02-17	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 81–193（113 aa） Fragment：C-TERMINAL LIM DOMAIN RESIDUES 82 - 194	Not recorded	ZN ZINC ION × 2	SOLUTION NMR NMR measurement conditions pH 7.2；299 K	Resolution not provided

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CSRP2_COTJA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–113； UniProt 82–194

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	1cxx
Deposition date deposition_date	1999-08-31
Structure title title	MUTANT R122A OF QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED STRUCTURE
Keywords keywords	LIM DOMAIN CONTAINING PROTEINS, METAL-BINDING PROTEIN, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	12.28 Å
Radius of gyration Rg (electron density) rg_electron	11.09 Å
Forward intensity I(0) i0	1132880.00
Molecular weight molecular_weight	6484.0 kDa
Excluded volume excluded_volume	7878 Å³
Envelope volume envelope_volume	8874 Å³
Hydration-shell volume shell_volume	7301 Å³
Envelope diameter envelope_diameter	40.7 Å
Shell Rg shell_rg	15.98 Å
Envelope Rg envelope_rg	11.50 Å
Shape Rg shape_rg	11.08 Å
Total Rg total_rg	12.41 Å
Total atoms total_atoms	868
Residues n_residues	59
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	42.7 Å
Rg (real space) rg_real	12.28 Å
Rg uncertainty (real space) rg_real_error	0.33 Å
I(0) (real space) i0_real	1.1330e+06
I(0) uncertainty (real space) i0_real_error	1.1700e+04
Rg (reciprocal space) rg_reciprocal	12.28 Å
I(0) (reciprocal space) i0_reciprocal	1133000.0000
Solution quality estimate total_estimate	0.8668
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	14.6 Å
Skewness Skewness skewness	0.358
Kurtosis Kurtosis kurtosis	-0.088
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	122200.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.776; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.981

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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) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1cxxa1
Class class	g — Small proteins
Fold Fold fold	g.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamily	g.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family family	g.39.1.3 — LIM domain

Domain ID domain_id	d1cxxa2
Class class	g — Small proteins
Fold Fold fold	g.39 — Glucocorticoid receptor-like (DNA-binding domain)
Superfamily Superfamily superfamily	g.39.1 — Glucocorticoid receptor-like (DNA-binding domain)
Family Family family	g.39.1.3 — LIM domain

CATH v4.4 (1 domains)

Domain ID domain_id	1cxxA00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	110 — Cysteine Rich Protein
Homologous superfamily homologous superfamily	10 — Cysteine Rich Protein

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8. Citations (1)

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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	CYSTEINE AND GLYCINE-RICH PROTEIN CRP2
Molecular weight formula_weight	12039.7 kDa
Mutation mutation	R122A
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	868

来源生物 organism	Coturnix japonica
通用名 common_name	Japanese quail
NCBI Class编号 ncbi_taxonomy_id	93934
宿主生物 host_organism	Escherichia coli

MUTANT R122A OF QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED STRUCTURE

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

CYSTEINE AND GLYCINE-RICH PROTEIN CRP2

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

fit	/app/data/saxs_computation/cx/1cxx/1cxx.fit
pddf	/app/data/pr_computation/cx/1cxx/1cxx.pr.out
profile	/app/data/saxs_computation/cx/1cxx/1cxx.dat