2mqw

Solution structure of a proteasome related subunit N terminal domain

Method: SOLUTION NMR Dmax: 78.2 Å Quality: REASONABLE

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

26S proteasome regulatory subunit RPN9

Saccharomyces cerevisiae S288c

UniProt Q04062

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 1–160 Fragment:N terminal domain, UNP RESIDUES 1-160 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 210;Pressure AMBIENT NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] Protein-1, 50 mM sodium phosphate-2, 100 mM sodium chloride-3, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5 mM [U-100% 15N] Protein-4, 50 mM sodium phosphate-5, 100 mM sodium chloride-6, 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.

32 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN9_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–163; UniProt 1–160

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 2mqw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2mqw
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2mqw
Deposition date deposition_date2014-06-30
Structure title titleSolution structure of a proteasome related subunit N terminal domain
Keywords keywordsA-HELIX BUNDLE, HYDROLASE; HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier20.13
Radius of gyration Rg (electron density) rg_electron19.86
Forward intensity I(0) i01847770000.00
Molecular weight molecular_weight377810.0 kDa
Excluded volume excluded_volume477730 ų
Envelope volume envelope_volume82933 ų
Hydration-shell volume shell_volume25942 ų
Envelope diameter envelope_diameter86.7
Shell Rg shell_rg33.34
Envelope Rg envelope_rg30.01
Shape Rg shape_rg19.79
Total Rg total_rg20.36
Total atoms total_atoms53280
Residues n_residues3200
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 dmax78.2
Rg (real space) rg_real20.39
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real1.8480e+09
I(0) uncertainty (real space) i0_real_error2.9940e+07
Rg (reciprocal space) rg_reciprocal20.34
I(0) (reciprocal space) i0_reciprocal1848000000.0000
Solution quality estimate total_estimate0.7384
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.9
Skewness Skewness skewness0.716
Kurtosis Kurtosis kurtosis0.316
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1282000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.401; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.439; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)