1x4a

Solution structure of RRM domain in splicing factor SF2

Method: SOLUTION NMR Dmax: 48.4 Å Quality: REASONABLE

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

splicing factor, arginine/serine-rich 1 (splicing factor 2, alternate splicing factor) variant

Homo sapiens

UniProt Q07955

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 33–128 Fragment:RRM domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:0.8mM U-15,13C; 20mM phosphate buffer NA; 100mM NaCl; 1mM d-DTT; 0.02% NaN3 | 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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SFRS1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–103; UniProt 33–128

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

SAXS profile for 1x4a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1x4a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1x4a
Deposition date deposition_date2005-05-14
Structure title titleSolution structure of RRM domain in splicing factor SF2
Keywords keywords;structure genomics, SURP domain, splicing factor SF2, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, RNA BINDING PROTEIN ;; RNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.43
Radius of gyration Rg (electron density) rg_electron16.40
Forward intensity I(0) i0906188000.00
Molecular weight molecular_weight234520.0 kDa
Excluded volume excluded_volume285550 ų
Envelope volume envelope_volume78373 ų
Hydration-shell volume shell_volume26445 ų
Envelope diameter envelope_diameter84.3
Shell Rg shell_rg32.15
Envelope Rg envelope_rg26.54
Shape Rg shape_rg16.31
Total Rg total_rg17.14
Total atoms total_atoms32000
Residues n_residues2180
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax48.4
Rg (real space) rg_real16.29
Rg uncertainty (real space) rg_real_error0.09
I(0) (real space) i0_real8.6530e+08
I(0) uncertainty (real space) i0_real_error8.1450e+06
Rg (reciprocal space) rg_reciprocal17.66
I(0) (reciprocal space) i0_reciprocal906200000.0000
Solution quality estimate total_estimate0.6733
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.4
Skewness Skewness skewness0.441
Kurtosis Kurtosis kurtosis-0.190
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha2.4380
Highest regularization parameter α highest_alpha922700.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.004; Oscil: 0.927; Stabil: 0.993; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1x4aa1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.1 — Canonical RBD
Domain ID domain_idd1x4aa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1x4aa3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1x4aA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain

8. Citations (1)

9. Files and Curves (10)