SAXSdb — 1joy

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

PROTEIN (ENVZ_ECOLI)

Escherichia coli

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 223–289 Chain B； UniProt 223–289	Fragment：RESIDUES 223-289	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 7.2；298 K	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 1JOY	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BXD NMR STRUCTURE OF THE HISTIDINE KINASE DOMAIN OF THE E. COLI OSMOSENSOR ENVZ Deposited 1998-10-02	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 290–450（161 aa） Fragment：RESIDUES 290-450	Not recorded	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1	SOLUTION NMR NMR measurement conditions pH 7；298 K	Resolution not provided

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

View Construct and Data Evidence

UniProt name	ENVZ_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–67； UniProt 223–289 Author chain B； PDBConstruct 1–67； UniProt 223–289

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	1joy
Deposition date deposition_date	1998-12-28
Structure title title	SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA COLI BY MULTI-DIMENSIONAL NMR.
Keywords keywords	HISTIDINE KINASE, SENSORY TRANSDUCTION, OSMOLARITY SENSOR PROTEIN, INNER MEMBRANE, PHOSPHORYLATION, TRANSFERASE; TRANSFERASE
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	31.11 Å
Radius of gyration Rg (electron density) rg_electron	30.55 Å
Forward intensity I(0) i0	1558280000.00
Molecular weight molecular_weight	318390.0 kDa
Excluded volume excluded_volume	394390 Å³
Envelope volume envelope_volume	237640 Å³
Hydration-shell volume shell_volume	55161 Å³
Envelope diameter envelope_diameter	118.8 Å
Shell Rg shell_rg	42.57 Å
Envelope Rg envelope_rg	35.20 Å
Shape Rg shape_rg	30.50 Å
Total Rg total_rg	31.12 Å
Total atoms total_atoms	44436
Residues n_residues	2814
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	108.4 Å
Rg (real space) rg_real	31.17 Å
Rg uncertainty (real space) rg_real_error	0.94 Å
I(0) (real space) i0_real	1.5580e+09
I(0) uncertainty (real space) i0_real_error	2.4810e+07
Rg (reciprocal space) rg_reciprocal	31.15 Å
I(0) (reciprocal space) i0_reciprocal	1558000000.0000
Solution quality estimate total_estimate	0.7919
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	34.0 Å
Skewness Skewness skewness	0.404
Kurtosis Kurtosis kurtosis	-0.245
Angular range angular_range	— – 0.2550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	63360000.0000
Real-space data points n_real_points	52
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.805; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.878; 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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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1joya_
Class class	a — All alpha proteins
Fold Fold fold	a.30 — ROP-like
Superfamily Superfamily superfamily	a.30.2 — Homodimeric domain of signal transducing histidine kinase
Family Family family	a.30.2.1 — Homodimeric domain of signal transducing histidine kinase

Domain ID domain_id	d1joyb_
Class class	a — All alpha proteins
Fold Fold fold	a.30 — ROP-like
Superfamily Superfamily superfamily	a.30.2 — Homodimeric domain of signal transducing histidine kinase
Family Family family	a.30.2.1 — Homodimeric domain of signal transducing histidine kinase

CATH v4.4 (2 domains)

Domain ID domain_id	1joyA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	130 — Signal transduction histidine kinase, dimerisation/phosphotransfer (DHp) domain

Domain ID domain_id	1joyB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	130 — Signal transduction histidine kinase, dimerisation/phosphotransfer (DHp) domain

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8. Citations (2)

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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	PROTEIN (ENVZ_ECOLI)
Molecular weight formula_weight	7593.7 kDa
EC 编号 ec_number	2.7.3.-
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	44436

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli BL21(DE3)

SOLUTION STRUCTURE OF THE HOMODIMERIC DOMAIN OF ENVZ FROM ESCHERICHIA COLI BY MULTI-DIMENSIONAL NMR.

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

PROTEIN (ENVZ_ECOLI)

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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/jo/1joy/1joy.fit
pddf	/app/data/pr_computation/jo/1joy/1joy.pr.out
profile	/app/data/saxs_computation/jo/1joy/1joy.dat