6y96

solution structure of cold-shock domain 9 of drosophila Upstream of N-Ras (Unr)

Method: SOLUTION NMR Dmax: 61.4 Å Quality: REASONABLE

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

Upstream of N-ras, isoform A

Drosophila melanogaster

UniProt Q9VSK3

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 899–990 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.8;298 K;Ionic strength (raw mmCIF value) 50;Pressure 1 NMR sample composition:0.24 mM [U-99% 13C; U-99% 15N] protein, 50 mM sodium phosphate, 50 mM sodium chloride, 1 mM DTT, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.24 mM [U-99% 13C; U-99% 15N] protein, 50 mM sodium phosphate, 50 mM sodium chloride, 1 mM DTT, 100% D2O | 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.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9VSK3_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–94; UniProt 899–990

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 6y96

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6y96
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6y96
Deposition date deposition_date2020-03-06
Structure title titlesolution structure of cold-shock domain 9 of drosophila Upstream of N-Ras (Unr)
Keywords keywordsCSD, RBP, 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_guinier14.14
Radius of gyration Rg (electron density) rg_electron13.89
Forward intensity I(0) i0631566000.00
Molecular weight molecular_weight204330.0 kDa
Excluded volume excluded_volume252890 ų
Envelope volume envelope_volume34915 ų
Hydration-shell volume shell_volume16113 ų
Envelope diameter envelope_diameter64.5
Shell Rg shell_rg24.97
Envelope Rg envelope_rg20.14
Shape Rg shape_rg13.86
Total Rg total_rg14.25
Total atoms total_atoms28600
Residues n_residues1880
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 dmax61.4
Rg (real space) rg_real14.21
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real6.3160e+08
I(0) uncertainty (real space) i0_real_error8.6430e+06
Rg (reciprocal space) rg_reciprocal14.21
I(0) (reciprocal space) i0_reciprocal631600000.0000
Solution quality estimate total_estimate0.6958
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.3
Skewness Skewness skewness0.588
Kurtosis Kurtosis kurtosis0.649
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha334600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.227; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.361; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6y96A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins

8. Citations (1)

9. Files and Curves (10)