2mor

A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings

Method: SOLUTION NMR Dmax: 51.2 Å Quality: REASONABLE

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

Ubiquitin

Homo sapiens

UniProt P0CG48

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 1–76 Fragment:UNP residues 1-76 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.6;292 K;Pressure ambient NMR measurement conditions:pH 6.6;298 K;Pressure ambient NMR measurement conditions:pH 6.6;304 K;Pressure ambient NMR sample composition:0.7 mM [U-13C; U-15N] Ubiquitin, 10 mM phosphate, 5 w/v DMPC:DHPC(3:1), 93% H2O/7% D2O | 93% H2O/7% 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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

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

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 2mor

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2mor
Deposition date deposition_date2014-04-29
Structure title titleA tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings
Keywords keywordsUbiquitin, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.62
Radius of gyration Rg (electron density) rg_electron11.89
Forward intensity I(0) i01601300.00
Molecular weight molecular_weight8565.0 kDa
Excluded volume excluded_volume10817 ų
Envelope volume envelope_volume12650 ų
Hydration-shell volume shell_volume9279 ų
Envelope diameter envelope_diameter46.3
Shell Rg shell_rg17.31
Envelope Rg envelope_rg12.37
Shape Rg shape_rg11.86
Total Rg total_rg13.39
Total atoms total_atoms1231
Residues n_residues76
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 dmax51.2
Rg (real space) rg_real13.55
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.6010e+06
I(0) uncertainty (real space) i0_real_error1.9360e+04
Rg (reciprocal space) rg_reciprocal13.56
I(0) (reciprocal space) i0_reciprocal1601000.0000
Solution quality estimate total_estimate0.7168
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.5
Skewness Skewness skewness0.232
Kurtosis Kurtosis kurtosis0.023
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha476400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.448; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

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_idd2mora_
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 (2)

9. Files and Curves (10)