2hj8

Solution NMR structure of the C-terminal domain of the interferon alpha-inducible ISG15 protein from Homo sapiens. Northeast Structural Genomics target HR2873B

Method: SOLUTION NMR Dmax: 40.5 Å Quality: GOOD

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

Interferon-induced 17 kDa protein

Homo sapiens

UniProt P05161

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 78–156 Fragment:ISG15 C-terminal domain (8.9 kDa), Ubiquitin-like 2 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;293 K;Ionic strength (raw mmCIF value) 50 mM ammonium citrate, 5 mM CaCl2;Pressure ambient NMR sample composition:0.81 mM U-13C,15N HR2873B, 50 mM ammonium citrate, 5 mM CaCl2, 1x protease inhibitor, 0.02% NaN3, pH 6.5, 5% D2O / 95% H2O | 5% D2O / 95% H2O NMR sample composition:0.9 mM 5%-13C,U-15N HR2873B, 50 mM ammonium citrate, 5 mM CaCl2, 1x protease inhibitor, 0.02% NaN3, pH 6.5, 5% D2O / 95% H2O | 5% D2O / 95% H2O 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.

21 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–80; UniProt 78–156

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 2hj8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2hj8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2hj8
Deposition date deposition_date2006-06-30
Structure title titleSolution NMR structure of the C-terminal domain of the interferon alpha-inducible ISG15 protein from Homo sapiens. Northeast Structural Genomics target HR2873B
Keywords keywordsHR2873B, human ISG15, Northeast Structural Genomics Consortium, Protein Structure Initiative, NESG, PSI-1, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.00
Radius of gyration Rg (electron density) rg_electron11.80
Forward intensity I(0) i0384441000.00
Molecular weight molecular_weight169970.0 kDa
Excluded volume excluded_volume214540 ų
Envelope volume envelope_volume19546 ų
Hydration-shell volume shell_volume12172 ų
Envelope diameter envelope_diameter47.1
Shell Rg shell_rg19.51
Envelope Rg envelope_rg13.90
Shape Rg shape_rg11.76
Total Rg total_rg12.09
Total atoms total_atoms24100
Residues n_residues1500
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 dmax40.5
Rg (real space) rg_real11.91
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real3.8440e+08
I(0) uncertainty (real space) i0_real_error4.3210e+06
Rg (reciprocal space) rg_reciprocal11.91
I(0) (reciprocal space) i0_reciprocal384400000.0000
Solution quality estimate total_estimate0.7549
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary16.4
Skewness Skewness skewness0.047
Kurtosis Kurtosis kurtosis-0.132
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha116900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.604; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2hj8a_
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.15.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id2hj8A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)