2m09

Structure, phosphorylation and U2AF65 binding of the Nterminal Domain of splicing factor 1 during 3 splice site Recognition

Method: SOLUTION NMR Dmax: 49.3 Å Quality: REASONABLE

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

Splicing factor 1

Homo sapiens

UniProt Q15637

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 27–145 Fragment:UNP residues 27-145 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 70;Pressure ambient NMR sample composition:100-600 uM [U-15N] protein, 100-600 uM [U-13C; U-15N] entity, 100-600 uM [U-13C; U-15N; U-2H] entity, 90% H2O/10% D2O | 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.

8 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SF01_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–121; UniProt 27–145

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 2m09

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2m09
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2m09
Deposition date deposition_date2012-10-22
Structure title titleStructure, phosphorylation and U2AF65 binding of the Nterminal Domain of splicing factor 1 during 3 splice site Recognition
Keywords keywordsspliceosome assembly, SF1, UHM, ULM, RRM, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.17
Radius of gyration Rg (electron density) rg_electron18.73
Forward intensity I(0) i0284252000.00
Molecular weight molecular_weight138020.0 kDa
Excluded volume excluded_volume172350 ų
Envelope volume envelope_volume60990 ų
Hydration-shell volume shell_volume22707 ų
Envelope diameter envelope_diameter94.2
Shell Rg shell_rg29.37
Envelope Rg envelope_rg23.93
Shape Rg shape_rg18.70
Total Rg total_rg19.30
Total atoms total_atoms19550
Residues n_residues1210
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 dmax49.3
Rg (real space) rg_real18.16
Rg uncertainty (real space) rg_real_error0.07
I(0) (real space) i0_real2.7100e+08
I(0) uncertainty (real space) i0_real_error2.1410e+06
Rg (reciprocal space) rg_reciprocal19.28
I(0) (reciprocal space) i0_reciprocal284200000.0000
Solution quality estimate total_estimate0.6851
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.607
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha3.1240
Highest regularization parameter α highest_alpha411600.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 1.000; Stabil: 0.976; Sysdev: 0.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)