2msg

Solid-state NMR structure of ubiquitin

Method: SOLID-STATE NMR Dmax: 41.1 Å Quality: GOOD

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

Ubiquitin

Homo sapiens

UniProt P0CG47

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 7–78 Fragment:UNP residuse 1-72 No other associated polymer SOLID-STATE NMR NMR measurement conditions:273 K;Pressure ambient NMR sample composition:20 mg [U-100% 13C; U-100% 15N] Ubiquitin, 30 mg [1-glucose 13C,U-100% 15N] Ubiquitin, 40 mg [2-glucose 13C,U-100% 15N] Ubiquitin, 40 % v/v MPD, 0.2 M CdCl2, 1 mg DSS, 100% H20 | 100% H20 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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–72; UniProt 7–78

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 2msg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2msg
Deposition date deposition_date2014-08-04
Structure title titleSolid-state NMR structure of ubiquitin
Keywords keywordsUBIQUITIN FOLD, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLID-STATE NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.92
Radius of gyration Rg (electron density) rg_electron11.39
Forward intensity I(0) i092176400.00
Molecular weight molecular_weight81804.0 kDa
Excluded volume excluded_volume103450 ų
Envelope volume envelope_volume17006 ų
Hydration-shell volume shell_volume11250 ų
Envelope diameter envelope_diameter42.5
Shell Rg shell_rg18.72
Envelope Rg envelope_rg13.15
Shape Rg shape_rg11.35
Total Rg total_rg11.81
Total atoms total_atoms11740
Residues n_residues720
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 dmax41.1
Rg (real space) rg_real11.82
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real9.2180e+07
I(0) uncertainty (real space) i0_real_error8.9530e+05
Rg (reciprocal space) rg_reciprocal11.83
I(0) (reciprocal space) i0_reciprocal92180000.0000
Solution quality estimate total_estimate0.8214
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.1
Skewness Skewness skewness-0.011
Kurtosis Kurtosis kurtosis-0.194
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha197400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.564; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)