SAXSdb — 1d8z

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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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 36–123	Fragment：FIRST RNA-BINDING DOMAIN (RBD1)	No other associated polymer	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

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 1D8Z	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1D9A SOLUTION STRUCTURE OF THE SECOND RNA-BINDING DOMAIN (RBD2) OF HU ANTIGEN C (HUC) Deposited 1999-10-26	Different construct	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
1FNX SOLUTION STRUCTURE OF THE HUC RBD1-RBD2 COMPLEXED WITH THE AU-RICH ELEMENT Deposited 2000-08-24	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain H 35–208（174 aa） Fragment：THE FIRST AND THE SECOND RNA-BINDING DOMAINS	Not recorded	No recorded non-water small molecule	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

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	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–89； UniProt 36–123

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	1d8z
Deposition date deposition_date	1999-10-26
Structure title title	SOLUTION STRUCTURE OF THE FIRST RNA-BINDING DOMAIN (RBD1) OF HU ANTIGEN C (HUC)
Keywords keywords	RNA-BINDING DOMAIN, RIKEN Structural Genomics/Proteomics Initiative, RSGI, Structural Genomics, RNA BINDING PROTEIN; RNA BINDING 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	15.36 Å
Radius of gyration Rg (electron density) rg_electron	14.05 Å
Forward intensity I(0) i0	2133970.00
Molecular weight molecular_weight	9838.0 kDa
Excluded volume excluded_volume	12301 Å³
Envelope volume envelope_volume	14851 Å³
Hydration-shell volume shell_volume	9679 Å³
Envelope diameter envelope_diameter	54.5 Å
Shell Rg shell_rg	19.04 Å
Envelope Rg envelope_rg	15.01 Å
Shape Rg shape_rg	13.98 Å
Total Rg total_rg	15.45 Å
Total atoms total_atoms	1387
Residues n_residues	89
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	55.7 Å
Rg (real space) rg_real	15.40 Å
Rg uncertainty (real space) rg_real_error	0.45 Å
I(0) (real space) i0_real	2.1340e+06
I(0) uncertainty (real space) i0_real_error	2.5050e+04
Rg (reciprocal space) rg_reciprocal	15.39 Å
I(0) (reciprocal space) i0_reciprocal	2134000.0000
Solution quality estimate total_estimate	0.6916
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	16.9 Å
Skewness Skewness skewness	0.417
Kurtosis Kurtosis kurtosis	-0.095
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	334500.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.679; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.846; Smooth: 0.999

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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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1d8za_
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

CATH v4.4 (1 domains)

Domain ID domain_id	1d8zA00
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	—

Description description	HU ANTIGEN C
Molecular weight formula_weight	9847.1 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	1387

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 BL21(DE3)

SOLUTION STRUCTURE OF THE FIRST RNA-BINDING DOMAIN (RBD1) OF HU ANTIGEN C (HUC)

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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/d8/1d8z/1d8z.fit
pddf	/app/data/pr_computation/d8/1d8z/1d8z.pr.out
profile	/app/data/saxs_computation/d8/1d8z/1d8z.dat