2mjb

Solution nmr structure of ubiquitin refined against dipolar couplings in 4 media

Method: SOLUTION NMR Dmax: 45.6 Å Quality: GOOD

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

Ubiquitin-60S ribosomal protein L40

Homo sapiens

UniProt P62987

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 229–304 Fragment:Ubiquitin-like 3 domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;308 K;Pressure ambient NMR measurement conditions:pH 6;298 K;Pressure ambient NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N; U-100% 2H] ubiquitin, 20 mM [U-100% 2H] D4-imidazole, 4.8 mM squalamine, 1.5 mM hexanol, 10 mM sodium phosphate, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N; U-100% 2H] ubiquitin, 20 mM [U-100% 2H] D4-imidazole, 1.5 mM hexanol, 10 mM sodium phosphate, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.6 mM [U-100% 13C; U-100% 15N] ubiquitin, 13 mg/mL Pf1 phage, 140 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.8 mM [U-100% 13C; U-100% 15N; U-100% 2H] ubiquitin, 14 mg/mL Pf1 phage, 150 mM sodium chloride, 95% H2O/5% D2O | 95% H2O/5% 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.

153 other PDB entries and 174 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL40_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–76; UniProt 229–304

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 2mjb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2mjb
Deposition date deposition_date2014-01-02
Structure title titleSolution nmr structure of ubiquitin refined against dipolar couplings in 4 media
Keywords keywordsRESIDUAL DIPOLAR COUPLING, SQUALAMINE, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.64
Radius of gyration Rg (electron density) rg_electron12.08
Forward intensity I(0) i0395344000.00
Molecular weight molecular_weight171300.0 kDa
Excluded volume excluded_volume216330 ų
Envelope volume envelope_volume16024 ų
Hydration-shell volume shell_volume10527 ų
Envelope diameter envelope_diameter51.9
Shell Rg shell_rg18.77
Envelope Rg envelope_rg14.28
Shape Rg shape_rg12.06
Total Rg total_rg12.31
Total atoms total_atoms24620
Residues n_residues1520
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 dmax45.6
Rg (real space) rg_real12.61
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real3.9530e+08
I(0) uncertainty (real space) i0_real_error4.6080e+06
Rg (reciprocal space) rg_reciprocal12.61
I(0) (reciprocal space) i0_reciprocal395300000.0000
Solution quality estimate total_estimate0.7882
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.5
Skewness Skewness skewness0.313
Kurtosis Kurtosis kurtosis0.424
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha159600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.421; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2mjba_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related

8. Citations (1)

9. Files and Curves (10)