SAXSdb — 1fnx

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

HU ANTIGEN C

Mus musculus

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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric（2） Consistent with all polymer counts	Chain H； UniProt 35–208	Fragment：THE FIRST AND THE SECOND RNA-BINDING DOMAINS	AU-RICH RNA ELEMENT × 1	SOLUTION NMR NMR measurement conditions：pH 6；298 K；Ionic strength (raw mmCIF value) 20mM；Pressure ambient NMR sample composition：20mM phosphate K buffer; 0.8mM RBD1-RBD2 U-15N,13C; 0.8mM ARE; 1mM DTT; 100 units/ml ribonuclease inhibitor \| 90% H2O/10% D2O NMR sample composition：20mM phosphate K buffer; 0.8mM RBD1-RBD2; 0.8mM ARE U-15N,13C; 1mM DTT; 100 units/ml ribonuclease inhibitor \| 90% H2O/10% D2O NMR sample composition：20mM phosphate K buffer; 0.8mM RBD1-RBD2; 0.8mM ARE U-15N,13C; 1mM DTT; 100 units/ml ribonuclease inhibitor \| 100% D2O NMR sample composition：20mM phosphate K buffer; 0.8mM RBD1-RBD2; 0.8mM ARE U-15N,13C-Adenosine; 1mM DTT; 100 units/ml ribonuclease inhibitor \| 90% H2O/10% D2O NMR sample composition：20mM phosphate K buffer; 0.8mM RBD1-RBD2; 0.8mM ARE U-15N,13C-Adenosine; 1mM DTT; 100 units/ml ribonuclease inhibitor \| 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.

Other PDB	Difference from Current Entry 1FNX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1D8Z SOLUTION STRUCTURE OF THE FIRST RNA-BINDING DOMAIN (RBD1) OF HU ANTIGEN C (HUC) Deposited 1999-10-26	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 36–123（88 aa） Fragment：FIRST RNA-BINDING DOMAIN (RBD1)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.6；298 K；Ionic strength (raw mmCIF value) 20 mM；Pressure AMBIENT NMR sample composition 2MM PROTEIN; 20 MM POTASSIUM OXALATE BUFFER; 90% H2O; 10% D2O NMR sample composition 2MM PROTEIN U-15N; 20 MM POTASSIUM OXALATE BUFFER; 90% H2O; 10% D2O	Resolution not provided
1D9A SOLUTION STRUCTURE OF THE SECOND RNA-BINDING DOMAIN (RBD2) OF HU ANTIGEN C (HUC) Deposited 1999-10-26	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 124–208（85 aa） Fragment：SECOND RNA-BINDING DOMAIN (RBD2)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.6；298 K；Ionic strength (raw mmCIF value) 20 mM；Pressure AMBIENT NMR sample composition 2MM PROTEIN; 20 MM POTASSIUM OXALATE BUFFER; 90% H2O; 10% D2O NMR sample composition 2MM PROTEIN U-15N; 20 MM POTASSIUM OXALATE BUFFER; 90% H2O; 10% D2O	Resolution not provided

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

View Construct and Data Evidence

UniProt name	ELAV3_MOUSE
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain H； PDBConstruct 1–174； UniProt 35–208

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	1fnx
Deposition date deposition_date	2000-08-24
Structure title title	SOLUTION STRUCTURE OF THE HUC RBD1-RBD2 COMPLEXED WITH THE AU-RICH ELEMENT
Keywords keywords	RNA-binding domain, protein-RNA complex, immune system-RNA COMPLEX; immune system/RNA
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	22.12 Å
Radius of gyration Rg (electron density) rg_electron	26.27 Å
Forward intensity I(0) i0	3687580000.00
Molecular weight molecular_weight	468250.0 kDa
Excluded volume excluded_volume	566800 Å³
Envelope volume envelope_volume	151340 Å³
Hydration-shell volume shell_volume	35191 Å³
Envelope diameter envelope_diameter	143.2 Å
Shell Rg shell_rg	36.12 Å
Envelope Rg envelope_rg	54.98 Å
Shape Rg shape_rg	26.26 Å
Total Rg total_rg	26.42 Å
Total atoms total_atoms	63462
Residues n_residues	3864
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	53.1 Å
Rg (real space) rg_real	17.75 Å
Rg uncertainty (real space) rg_real_error	0.09 Å
I(0) (real space) i0_real	3.3740e+09
I(0) uncertainty (real space) i0_real_error	3.3310e+07
Rg (reciprocal space) rg_reciprocal	25.25 Å
I(0) (reciprocal space) i0_reciprocal	3685000000.0000
Solution quality estimate total_estimate	0.6840
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	20.6 Å
Skewness Skewness skewness	0.334
Kurtosis Kurtosis kurtosis	-0.315
Angular range angular_range	— – 0.3600 Å⁻¹
Current regularization parameter α current_alpha	2.9150
Highest regularization parameter α highest_alpha	11480000.0000
Real-space data points n_real_points	68
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.036; Oscil: 0.951; Stabil: 0.990; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.073

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	AU-RICH RNA ELEMENT
Molecular weight formula_weight	3062.8 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polyribonucleotide
Chain IDs strand_id	R
Atom count atom_count	63462

UAUUUAUUUU

Entity 2 Entity 2 polymer

Description description	HU ANTIGEN C
Molecular weight formula_weight	19180.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

MDSKTNLIVNYLPQNMTQDEFKSLFGSIGDIESCKLVRDKITGQSLGYGFVNYSDPNDADKAINTLNGLKLQTKTIKVSYARPSSASIRDANLYVSGLPKTMSQKEMEQLFSQYGRIITSRILLDQATGVSRGVGFIRFDKRIEAEEAIKGLNGQKPLGAAEPITVKFANNPSQ

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

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7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1fnxh1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family family	d.58.7.1 — Canonical RBD

Domain ID domain_id	d1fnxh2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family family	d.58.7.1 — Canonical RBD

Domain ID domain_id	d1fnxh3
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id	1fnxH01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	330 — RRM (RNA recognition motif) domain

Domain ID domain_id	1fnxH02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	330 — RRM (RNA recognition motif) domain

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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	—

fit	/app/data/saxs_computation/fn/1fnx/1fnx.fit
pddf	/app/data/pr_computation/fn/1fnx/1fnx.pr.out
profile	/app/data/saxs_computation/fn/1fnx/1fnx.dat

SOLUTION STRUCTURE OF THE HUC RBD1-RBD2 COMPLEXED WITH THE AU-RICH ELEMENT

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

HU ANTIGEN C

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

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)